anno_start	anno_end	anno_text	entity_type	sentence	section
0	9	Structure	evidence	Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf	TITLE
27	30	Wnt	protein_type	Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf	TITLE
41	48	Kremen1	protein	Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf	TITLE
97	101	LRP6	protein	Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf	TITLE
106	114	Dickkopf	protein_type	Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf	TITLE
0	14	Kremen 1 and 2	protein_type	Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling.	ABSTRACT
39	51	co-receptors	protein_type	Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling.	ABSTRACT
56	64	Dickkopf	protein_type	Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling.	ABSTRACT
66	69	Dkk	protein_type	Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling.	ABSTRACT
124	127	Wnt	protein_type	Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling.	ABSTRACT
22	40	crystal structures	evidence	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
48	58	ectodomain	structure_element	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
62	67	human	species	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
68	75	Kremen1	protein	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
77	81	KRM1	protein	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
81	84	ECD	structure_element	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
124	128	KRM1	protein	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
128	131	ECD	structure_element	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
198	220	triangular arrangement	protein_state	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
228	235	Kringle	structure_element	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
237	240	WSC	structure_element	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
246	249	CUB	structure_element	We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains.	ABSTRACT
4	14	structures	evidence	The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor.	ABSTRACT
53	56	WSC	structure_element	The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor.	ABSTRACT
67	91	hepatocyte growth factor	protein_type	The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor.	ABSTRACT
80	83	Wnt	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
84	95	co-receptor	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
96	102	Lrp5/6	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
104	107	Dkk	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
113	116	Krm	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
159	176	crystal structure	evidence	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
185	221	β-propeller/EGF repeats (PE) 3 and 4	structure_element	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
229	232	Wnt	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
233	244	co-receptor	protein_type	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
245	249	LRP6	protein	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
251	255	LRP6	protein	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
255	261	PE3PE4	structure_element	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
268	290	cysteine-rich domain 2	structure_element	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
292	296	CRD2	structure_element	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
301	305	DKK1	protein	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
311	315	KRM1	protein	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
315	318	ECD	structure_element	We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD.	ABSTRACT
0	4	DKK1	protein	DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC.	ABSTRACT
4	8	CRD2	structure_element	DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC.	ABSTRACT
31	35	LRP6	protein	DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC.	ABSTRACT
35	38	PE3	structure_element	DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC.	ABSTRACT
43	47	KRM1	protein	DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC.	ABSTRACT
47	58	Kringle-WSC	structure_element	DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC.	ABSTRACT
0	8	Modeling	experimental_method	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
30	55	surface plasmon resonance	experimental_method	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
73	89	interaction site	site	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
98	102	Krm1	protein	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
102	105	CUB	structure_element	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
110	114	Lrp6	protein	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
114	117	PE2	structure_element	Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.	ABSTRACT
4	13	structure	evidence	The structure of the KREMEN 1 ectodomain is solved from three crystal forms	ABSTRACT
21	29	KREMEN 1	protein	The structure of the KREMEN 1 ectodomain is solved from three crystal forms	ABSTRACT
30	40	ectodomain	structure_element	The structure of the KREMEN 1 ectodomain is solved from three crystal forms	ABSTRACT
44	50	solved	experimental_method	The structure of the KREMEN 1 ectodomain is solved from three crystal forms	ABSTRACT
62	75	crystal forms	evidence	The structure of the KREMEN 1 ectodomain is solved from three crystal forms	ABSTRACT
0	7	Kringle	structure_element	Kringle, WSC, and CUB subdomains interact tightly to form a single structural unit	ABSTRACT
9	12	WSC	structure_element	Kringle, WSC, and CUB subdomains interact tightly to form a single structural unit	ABSTRACT
18	21	CUB	structure_element	Kringle, WSC, and CUB subdomains interact tightly to form a single structural unit	ABSTRACT
4	13	interface	site	The interface to DKKs is formed from the Kringle and WSC domains	ABSTRACT
17	21	DKKs	protein_type	The interface to DKKs is formed from the Kringle and WSC domains	ABSTRACT
41	48	Kringle	structure_element	The interface to DKKs is formed from the Kringle and WSC domains	ABSTRACT
53	56	WSC	structure_element	The interface to DKKs is formed from the Kringle and WSC domains	ABSTRACT
4	7	CUB	structure_element	The CUB domain is found to interact directly with LRP6PE1PE2	ABSTRACT
50	54	LRP6	protein	The CUB domain is found to interact directly with LRP6PE1PE2	ABSTRACT
54	60	PE1PE2	structure_element	The CUB domain is found to interact directly with LRP6PE1PE2	ABSTRACT
28	38	ectodomain	structure_element	Zebisch et al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family.	ABSTRACT
39	48	structure	evidence	Zebisch et al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family.	ABSTRACT
52	60	KREMEN 1	protein	Zebisch et al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family.	ABSTRACT
64	72	receptor	protein_type	Zebisch et al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family.	ABSTRACT
77	80	Wnt	protein_type	Zebisch et al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family.	ABSTRACT
100	103	DKK	protein_type	Zebisch et al. describe the ectodomain structure of KREMEN 1, a receptor for Wnt antagonists of the DKK family.	ABSTRACT
0	3	Apo	protein_state	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
4	14	structures	evidence	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
21	33	complex with	protein_state	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
34	54	functional fragments	protein_state	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
58	62	DKK1	protein	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
67	71	LRP6	protein	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
130	133	Wnt	protein_type	Apo structures and a complex with functional fragments of DKK1 and LRP6 shed light on the function of this dual-mode regulator of Wnt signaling.	ABSTRACT
13	16	Wnt	protein_type	Signaling by Wnt morphogens is renowned for its fundamental roles in embryonic development, tissue homeostasis, and stem cell maintenance.	INTRO
68	71	Wnt	protein_type	Due to these functions, generation, delivery, and interpretation of Wnt signals are all heavily regulated in the animal body.	INTRO
0	10	Vertebrate	taxonomy_domain	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
11	19	Dickkopf	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
30	34	Dkk1	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
36	37	2	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
43	44	4	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
86	89	Wnt	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
129	132	Wnt	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
133	144	co-receptor	protein_type	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
145	151	LRP5/6	protein	Vertebrate Dickkopf proteins (Dkk1, 2, and 4) are one of many secreted antagonists of Wnt and function by blocking access to the Wnt co-receptor LRP5/6.	INTRO
0	6	Kremen	protein_type	Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk.	INTRO
17	21	Krm1	protein_type	Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk.	INTRO
26	30	Krm2	protein_type	Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk.	INTRO
81	104	transmembrane receptors	protein_type	Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk.	INTRO
109	112	Dkk	protein_type	Kremen proteins (Krm1 and Krm2) have been identified as additional high-affinity transmembrane receptors for Dkk.	INTRO
0	3	Krm	protein_type	Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning.	INTRO
8	11	Dkk	protein_type	Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning.	INTRO
25	28	Wnt	protein_type	Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning.	INTRO
47	54	Xenopus	taxonomy_domain	Krm and Dkk synergize in Wnt inhibition during Xenopus embryogenesis to regulate anterior-posterior patterning.	INTRO
43	54	presence of	protein_state	Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed.	INTRO
55	58	Dkk	protein_type	Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed.	INTRO
60	63	Krm	protein_type	Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed.	INTRO
80	92	complex with	protein_state	Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed.	INTRO
93	97	Lrp6	protein_type	Mechanistically it is thought that, in the presence of Dkk, Krm forms a ternary complex with Lrp6, which is then rapidly endocytosed.	INTRO
29	32	Wnt	protein_type	This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor.	INTRO
58	61	Dkk	protein_type	This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor.	INTRO
111	114	Wnt	protein_type	This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor.	INTRO
115	126	co-receptor	protein_type	This amplifies the intrinsic Wnt antagonistic activity of Dkk by efficiently depleting the cell surface of the Wnt co-receptor.	INTRO
25	29	Krm1	protein_type	In accordance with this, Krm1−/− and Krm2−/− double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits.	INTRO
37	41	Krm2	protein_type	In accordance with this, Krm1−/− and Krm2−/− double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits.	INTRO
45	60	double knockout	experimental_method	In accordance with this, Krm1−/− and Krm2−/− double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits.	INTRO
61	65	mice	taxonomy_domain	In accordance with this, Krm1−/− and Krm2−/− double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits.	INTRO
119	122	Wnt	protein_type	In accordance with this, Krm1−/− and Krm2−/− double knockout mice show a high bone mass phenotype typical of increased Wnt signaling, as well as growth of ectopic forelimb digits.	INTRO
69	72	dkk	protein_type	Growth of ectopic digits is further enhanced upon additional loss of dkk expression.	INTRO
4	7	Wnt	protein_type	The Wnt antagonistic activity of Krm1 is also linked to its importance for correct thymus epithelium formation in mice.	INTRO
33	37	Krm1	protein_type	The Wnt antagonistic activity of Krm1 is also linked to its importance for correct thymus epithelium formation in mice.	INTRO
114	118	mice	taxonomy_domain	The Wnt antagonistic activity of Krm1 is also linked to its importance for correct thymus epithelium formation in mice.	INTRO
18	24	intact	protein_state	The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia.	INTRO
25	29	KRM1	protein	The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia.	INTRO
41	46	human	species	The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia.	INTRO
141	151	ectodomain	structure_element	The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia.	INTRO
155	159	KRM1	protein	The importance of intact KRM1 for normal human development and health is highlighted by the recent finding that a homozygous mutation in the ectodomain of KRM1 leads to severe ectodermal dysplasia including oligodontia.	INTRO
19	22	Wnt	protein_type	Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators.	INTRO
48	51	Krm	protein_type	Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators.	INTRO
78	81	Krm	protein_type	Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators.	INTRO
114	117	Wnt	protein_type	Interestingly, the Wnt antagonistic activity of Krm is context dependent, and Krm proteins are actually dual-mode Wnt regulators.	INTRO
7	17	absence of	protein_state	In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling.	INTRO
18	21	Dkk	protein_type	In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling.	INTRO
23	27	Krm1	protein_type	In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling.	INTRO
32	33	2	protein_type	In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling.	INTRO
90	94	Lrp6	protein_type	In the absence of Dkk, Krm1 and 2 change their function from inhibition to enhancement of Lrp6-mediated signaling.	INTRO
21	25	Lrp6	protein_type	By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability.	INTRO
34	45	ectodomains	structure_element	By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability.	INTRO
47	50	Krm	protein_type	By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability.	INTRO
68	72	Lrp6	protein_type	By direct binding to Lrp6 via the ectodomains, Krm proteins promote Lrp6 cell-surface localization and hence increase receptor availability.	INTRO
37	40	Krm	protein_type	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
83	87	Krm1	protein_type	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
97	101	Krm2	protein_type	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
133	139	LRP5/6	protein	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
144	147	Wnt	protein_type	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
202	210	bound to	protein_state	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
211	214	Dkk	protein_type	Further increasing the complexity of Krm functionality, it was recently found that Krm1 (but not Krm2) can also act independently of LRP5/6 and Wnt as a dependence receptor, triggering apoptosis unless bound to Dkk.	INTRO
14	18	Krm1	protein_type	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
23	24	2	protein_type	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
29	58	type I transmembrane proteins	protein_type	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
73	83	ectodomain	structure_element	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
90	98	flexible	protein_state	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
99	115	cytoplasmic tail	structure_element	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
130	132	60	residue_range	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
133	135	75	residue_range	Structurally, Krm1 and 2 are type I transmembrane proteins with a 40 kDa ectodomain and a flexible cytoplasmic tail consisting of 60–75 residues.	INTRO
4	14	ectodomain	structure_element	The ectodomain consists of three similarly sized structural domains of around 10 kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold.	INTRO
106	113	Kringle	structure_element	The ectodomain consists of three similarly sized structural domains of around 10 kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold.	INTRO
122	124	KR	structure_element	The ectodomain consists of three similarly sized structural domains of around 10 kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold.	INTRO
143	146	WSC	structure_element	The ectodomain consists of three similarly sized structural domains of around 10 kDa each: the N-terminal Kringle domain (KR) is followed by a WSC domain of unknown fold.	INTRO
33	36	CUB	structure_element	The third structural domain is a CUB domain.	INTRO
3	27	approximately 70-residue	residue_range	An approximately 70-residue linker connects the CUB domain to the transmembrane span.	INTRO
28	34	linker	structure_element	An approximately 70-residue linker connects the CUB domain to the transmembrane span.	INTRO
48	51	CUB	structure_element	An approximately 70-residue linker connects the CUB domain to the transmembrane span.	INTRO
66	84	transmembrane span	structure_element	An approximately 70-residue linker connects the CUB domain to the transmembrane span.	INTRO
3	9	intact	protein_state	An intact KR-WSC-CUB domain triplet and membrane attachment is required for Wnt antagonism.	INTRO
10	20	KR-WSC-CUB	structure_element	An intact KR-WSC-CUB domain triplet and membrane attachment is required for Wnt antagonism.	INTRO
76	79	Wnt	protein_type	An intact KR-WSC-CUB domain triplet and membrane attachment is required for Wnt antagonism.	INTRO
4	22	transmembrane span	structure_element	The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism.	INTRO
27	43	cytoplasmic tail	structure_element	The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism.	INTRO
67	70	GPI	structure_element	The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism.	INTRO
71	77	linker	structure_element	The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism.	INTRO
96	99	Wnt	protein_type	The transmembrane span and cytoplasmic tail can be replaced with a GPI linker without impact on Wnt antagonism.	INTRO
4	14	structures	evidence	The structures presented here reveal the unknown fold of the WSC domain and the tight interactions of all three domains.	INTRO
61	64	WSC	structure_element	The structures presented here reveal the unknown fold of the WSC domain and the tight interactions of all three domains.	INTRO
58	85	LRP6PE3PE4-DKK1CRD2-KRM1ECD	complex_assembly	We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion.	INTRO
128	131	Wnt	protein_type	We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion.	INTRO
132	150	inhibitory complex	complex_assembly	We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion.	INTRO
165	169	Lrp6	protein	We further succeeded in determination of a low-resolution LRP6PE3PE4-DKK1CRD2-KRM1ECD complex, defining the architecture of the Wnt inhibitory complex that leads to Lrp6 cell-surface depletion.	INTRO
34	54	extracellular domain	structure_element	The recombinant production of the extracellular domain of Krm for structural studies proved challenging (see Experimental Procedures).	RESULTS
58	61	Krm	protein_type	The recombinant production of the extracellular domain of Krm for structural studies proved challenging (see Experimental Procedures).	RESULTS
66	84	structural studies	experimental_method	The recombinant production of the extracellular domain of Krm for structural studies proved challenging (see Experimental Procedures).	RESULTS
26	30	KRM1	protein	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
30	33	ECD	structure_element	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
34	48	complexes with	protein_state	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
49	55	DKK1fl	protein	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
57	61	DKK1	protein	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
61	72	Linker-CRD2	structure_element	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
78	82	DKK1	protein	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
82	86	CRD2	structure_element	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
124	138	gel filtration	experimental_method	We succeeded in purifying KRM1ECD complexes with DKK1fl, DKK1Linker-CRD2, and DKK1CRD2 that were monodisperse and stable in gel filtration, hence indicating at least micromolar affinity (data not shown).	RESULTS
8	21	crystal forms	evidence	Several crystal forms were obtained from these complexes, however, crystals always contained only KRM1 protein.	RESULTS
67	75	crystals	evidence	Several crystal forms were obtained from these complexes, however, crystals always contained only KRM1 protein.	RESULTS
98	102	KRM1	protein	Several crystal forms were obtained from these complexes, however, crystals always contained only KRM1 protein.	RESULTS
3	9	solved	experimental_method	We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2 Å resolution (Table 1).	RESULTS
14	23	structure	evidence	We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2 Å resolution (Table 1).	RESULTS
27	31	KRM1	protein	We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2 Å resolution (Table 1).	RESULTS
31	34	ECD	structure_element	We solved the structure of KRM1ECD in three crystal forms at 1.9, 2.8, and 3.2 Å resolution (Table 1).	RESULTS
20	29	structure	evidence	The high-resolution structure is a near full-length model (Figure 1).	RESULTS
40	51	full-length	protein_state	The high-resolution structure is a near full-length model (Figure 1).	RESULTS
4	9	small	protein_state	The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III.	RESULTS
11	19	flexible	protein_state	The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III.	RESULTS
25	32	charged	protein_state	The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III.	RESULTS
33	48	98AEHED102 loop	structure_element	The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III.	RESULTS
102	111	structure	evidence	The small, flexible, and charged 98AEHED102 loop could only be modeled in a slightly lower resolution structure and in crystal form III.	RESULTS
4	6	KR	structure_element	The KR, WSC, and CUB are arranged in a roughly triangular fashion with tight interactions between all three domains.	RESULTS
8	11	WSC	structure_element	The KR, WSC, and CUB are arranged in a roughly triangular fashion with tight interactions between all three domains.	RESULTS
17	20	CUB	structure_element	The KR, WSC, and CUB are arranged in a roughly triangular fashion with tight interactions between all three domains.	RESULTS
4	6	KR	structure_element	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
43	62	glycosylation sites	site	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
93	110	disulfide bridges	ptm	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
112	115	C32	residue_name_number	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
116	120	C114	residue_name_number	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
122	125	C55	residue_name_number	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
126	129	C95	residue_name_number	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
131	134	C84	residue_name_number	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
135	139	C109	residue_name_number	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
157	164	Kringle	structure_element	The KR domain, which bears two of the four glycosylation sites, contains the canonical three disulfide bridges (C32-C114, C55-C95, C84-C109) and, like other Kringle domains, is low in secondary structure elements.	RESULTS
30	37	Kringle	structure_element	The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7 Å for 73 aligned Cα (Figure 1B).	RESULTS
56	61	human	species	The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7 Å for 73 aligned Cα (Figure 1B).	RESULTS
62	73	plasminogen	protein	The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7 Å for 73 aligned Cα (Figure 1B).	RESULTS
94	120	root-mean-square deviation	evidence	The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7 Å for 73 aligned Cα (Figure 1B).	RESULTS
122	126	RMSD	evidence	The structurally most similar Kringle domain is that of human plasminogen (PDB: 1PKR) with an root-mean-square deviation (RMSD) of 1.7 Å for 73 aligned Cα (Figure 1B).	RESULTS
4	8	KRM1	protein	The KRM1 structure reveals the fold of the WSC domain for the first time.	RESULTS
9	18	structure	evidence	The KRM1 structure reveals the fold of the WSC domain for the first time.	RESULTS
43	46	WSC	structure_element	The KRM1 structure reveals the fold of the WSC domain for the first time.	RESULTS
4	13	structure	evidence	The structure is best described as a sandwich of a β1-β5-β3-β4-β2 antiparallel β sheet and a single α helix.	RESULTS
37	45	sandwich	structure_element	The structure is best described as a sandwich of a β1-β5-β3-β4-β2 antiparallel β sheet and a single α helix.	RESULTS
51	86	β1-β5-β3-β4-β2 antiparallel β sheet	structure_element	The structure is best described as a sandwich of a β1-β5-β3-β4-β2 antiparallel β sheet and a single α helix.	RESULTS
100	107	α helix	structure_element	The structure is best described as a sandwich of a β1-β5-β3-β4-β2 antiparallel β sheet and a single α helix.	RESULTS
4	13	structure	evidence	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
30	35	loops	structure_element	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
62	79	disulfide bridges	ptm	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
81	85	C122	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
86	90	C186	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
92	96	C147	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
97	101	C167	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
103	107	C151	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
108	112	C169	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
114	118	C190	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
119	123	C198	residue_name_number	The structure is also rich in loops and is stabilized by four disulfide bridges (C122-C186, C147-C167, C151-C169, C190-C198).	RESULTS
10	25	PDBeFold server	experimental_method	Using the PDBeFold server, we detected a surprising yet significant homology to PAN module domains.	RESULTS
80	98	PAN module domains	structure_element	Using the PDBeFold server, we detected a surprising yet significant homology to PAN module domains.	RESULTS
35	59	hepatocyte growth factor	protein_type	The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3 Å for 58 aligned Cα (Figure 1B).	RESULTS
61	64	HGF	protein_type	The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3 Å for 58 aligned Cα (Figure 1B).	RESULTS
84	94	superposes	experimental_method	The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3 Å for 58 aligned Cα (Figure 1B).	RESULTS
103	107	RMSD	evidence	The closest structural relative is hepatocyte growth factor (HGF, PDB: 1GP9), which superposes with an RMSD of 2.3 Å for 58 aligned Cα (Figure 1B).	RESULTS
4	7	CUB	structure_element	The CUB domain bears two glycosylation sites.	RESULTS
25	44	glycosylation sites	site	The CUB domain bears two glycosylation sites.	RESULTS
37	53	electron density	evidence	Although present, the quality of the electron density around N217 did not allow modeling of the sugar moiety.	RESULTS
61	65	N217	residue_name_number	Although present, the quality of the electron density around N217 did not allow modeling of the sugar moiety.	RESULTS
3	17	crystal form I	evidence	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
21	28	calcium	chemical	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
70	84	coordinated by	bond_interaction	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
105	109	D263	residue_name_number	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
111	115	D266	residue_name_number	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
133	137	D306	residue_name_number	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
166	170	N309	residue_name_number	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
177	182	water	chemical	In crystal form I, a calcium ion is present at the canonical position coordinated by the carboxylates of D263, D266 (bidentate), and D306, as well as the carbonyl of N309 and a water molecule.	RESULTS
4	23	coordination sphere	site	The coordination sphere deviates significantly from perfectly octahedral (not shown).	RESULTS
72	79	calcium	chemical	This might result in the site having a low affinity and may explain why calcium is not present in the two low-resolution crystal forms.	RESULTS
121	134	crystal forms	evidence	This might result in the site having a low affinity and may explain why calcium is not present in the two low-resolution crystal forms.	RESULTS
0	7	Loss of	protein_state	Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms.	RESULTS
8	15	calcium	chemical	Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms.	RESULTS
27	31	loop	structure_element	Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms.	RESULTS
77	90	crystal forms	evidence	Loss of calcium has led to loop rearrangements and partial disorder in these crystal forms.	RESULTS
39	44	CUB_C	structure_element	The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6 Å for 104 Cα (Figure 1B).	RESULTS
55	60	Tsg-6	protein	The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6 Å for 104 Cα (Figure 1B).	RESULTS
80	90	superposes	experimental_method	The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6 Å for 104 Cα (Figure 1B).	RESULTS
96	99	KRM	protein	The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6 Å for 104 Cα (Figure 1B).	RESULTS
99	102	CUB	structure_element	The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6 Å for 104 Cα (Figure 1B).	RESULTS
111	115	RMSD	evidence	The closest structural relative is the CUB_C domain of Tsg-6 (PDB: 2WNO), which superposes with KRMCUB with an RMSD of 1.6 Å for 104 Cα (Figure 1B).	RESULTS
2	15	superposition	experimental_method	A superposition of the three KRM1 structures reveals no major structural differences (Figure 1C) as anticipated from the plethora of interactions between the three domains.	RESULTS
29	33	KRM1	protein	A superposition of the three KRM1 structures reveals no major structural differences (Figure 1C) as anticipated from the plethora of interactions between the three domains.	RESULTS
34	44	structures	evidence	A superposition of the three KRM1 structures reveals no major structural differences (Figure 1C) as anticipated from the plethora of interactions between the three domains.	RESULTS
52	69	Ca2+ binding site	site	Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain.	RESULTS
73	97	crystal forms II and III	evidence	Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain.	RESULTS
102	106	loop	structure_element	Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain.	RESULTS
126	128	KR	structure_element	Minor differences are caused by the collapse of the Ca2+ binding site in crystal forms II and III and loop flexibility in the KR domain.	RESULTS
4	9	F207S	mutant	The F207S mutation recently found to cause ectodermal dysplasia in Palestinian families maps to the hydrophobic core of the protein at the interface of the three subdomains (Figure 1A).	RESULTS
100	116	hydrophobic core	site	The F207S mutation recently found to cause ectodermal dysplasia in Palestinian families maps to the hydrophobic core of the protein at the interface of the three subdomains (Figure 1A).	RESULTS
139	148	interface	site	The F207S mutation recently found to cause ectodermal dysplasia in Palestinian families maps to the hydrophobic core of the protein at the interface of the three subdomains (Figure 1A).	RESULTS
19	27	bound to	protein_state	Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity.	RESULTS
74	78	KRM1	protein	Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity.	RESULTS
110	113	Wnt	protein_type	Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity.	RESULTS
128	131	Wnt	protein_type	Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity.	RESULTS
149	152	Wnt	protein_type	Such a mutation is bound to severely destabilize the protein structure of KRM1, leading to disturbance of its Wnt antagonistic, Wnt stimulatory, and Wnt independent activity.	RESULTS
0	18	Co-crystallization	experimental_method	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
22	26	LRP6	protein	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
26	32	PE3PE4	structure_element	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
38	42	DKK1	protein	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
42	46	CRD2	structure_element	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
52	56	LRP6	protein	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
56	59	PE1	structure_element	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
90	94	DKK1	protein	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
148	151	Wnt	protein_type	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
166	169	Dkk	protein_type	Co-crystallization of LRP6PE3PE4 with DKK1CRD2, and LRP6PE1 with an N-terminal peptide of DKK1 has provided valuable structural insight into direct Wnt inhibition by Dkk ligands.	RESULTS
23	27	flat	protein_state	One face of the rather flat DKK1CRD2 fragment binds to the third β propeller of LRP6.	RESULTS
28	32	DKK1	protein	One face of the rather flat DKK1CRD2 fragment binds to the third β propeller of LRP6.	RESULTS
32	36	CRD2	structure_element	One face of the rather flat DKK1CRD2 fragment binds to the third β propeller of LRP6.	RESULTS
46	54	binds to	protein_state	One face of the rather flat DKK1CRD2 fragment binds to the third β propeller of LRP6.	RESULTS
59	76	third β propeller	structure_element	One face of the rather flat DKK1CRD2 fragment binds to the third β propeller of LRP6.	RESULTS
80	84	LRP6	protein	One face of the rather flat DKK1CRD2 fragment binds to the third β propeller of LRP6.	RESULTS
0	19	Mutational analyses	experimental_method	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
45	49	LRP6	protein	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
49	52	PE3	structure_element	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
69	73	DKK1	protein	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
73	77	CRD2	structure_element	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
88	104	Krm binding site	site	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
127	130	Dkk	protein_type	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
148	157	receptors	protein_type	Mutational analyses further implied that the LRP6PE3-averted face of DKK1CRD2 bears the Krm binding site, hence suggesting how Dkk can recruit both receptors into a ternary complex.	RESULTS
59	65	Lrp5/6	protein_type	To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials.	RESULTS
67	70	Dkk	protein_type	To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials.	RESULTS
76	79	Krm	protein_type	To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials.	RESULTS
97	122	LRP6PE3PE4-DKK1fl-KRM1ECD	complex_assembly	To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials.	RESULTS
134	156	crystallization trials	experimental_method	To obtain direct insight into ternary complex formation by Lrp5/6, Dkk, and Krm, we subjected an LRP6PE3PE4-DKK1fl-KRM1ECD complex to crystallization trials.	RESULTS
0	16	Diffraction data	evidence	Diffraction data collected from the resulting crystals were highly anisotropic with diffraction extending in the best directions to 3.5 Å and 3.7 Å but only to 6.4 Å in the third direction.	RESULTS
46	54	crystals	evidence	Diffraction data collected from the resulting crystals were highly anisotropic with diffraction extending in the best directions to 3.5 Å and 3.7 Å but only to 6.4 Å in the third direction.	RESULTS
36	47	diffraction	evidence	Despite the lack of high-resolution diffraction, the general architecture of the ternary complex is revealed (Figure 2A).	RESULTS
0	4	DKK1	protein	DKK1CRD2 binds to the top face of the LRP6 PE3 β propeller as described earlier for the binary complex.	RESULTS
4	8	CRD2	structure_element	DKK1CRD2 binds to the top face of the LRP6 PE3 β propeller as described earlier for the binary complex.	RESULTS
9	17	binds to	protein_state	DKK1CRD2 binds to the top face of the LRP6 PE3 β propeller as described earlier for the binary complex.	RESULTS
38	42	LRP6	protein	DKK1CRD2 binds to the top face of the LRP6 PE3 β propeller as described earlier for the binary complex.	RESULTS
43	46	PE3	structure_element	DKK1CRD2 binds to the top face of the LRP6 PE3 β propeller as described earlier for the binary complex.	RESULTS
47	58	β propeller	structure_element	DKK1CRD2 binds to the top face of the LRP6 PE3 β propeller as described earlier for the binary complex.	RESULTS
0	4	KRM1	protein	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
4	7	ECD	structure_element	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
20	27	bind on	protein_state	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
49	53	DKK1	protein	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
53	57	CRD2	structure_element	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
72	74	KR	structure_element	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
79	82	WSC	structure_element	KRM1ECD does indeed bind on the opposite side of DKK1CRD2 with only its KR and WSC domains engaged in binding (Figure 2A).	RESULTS
45	60	crystallization	experimental_method	Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linker (L).	RESULTS
76	83	density	evidence	Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linker (L).	RESULTS
109	113	CRD1	structure_element	Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linker (L).	RESULTS
121	134	domain linker	structure_element	Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linker (L).	RESULTS
136	137	L	structure_element	Although present in the complex subjected to crystallization, we observe no density that could correspond to CRD1 or the domain linker (L).	RESULTS
20	24	CRD2	structure_element	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
28	32	DKK1	protein	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
75	79	KRM1	protein	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
84	109	surface plasmon resonance	experimental_method	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
111	114	SPR	experimental_method	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
144	152	affinity	evidence	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
161	172	full-length	protein_state	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
173	177	DKK1	protein	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
194	198	KRM1	protein	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
198	201	ECD	structure_element	We confirm that the CRD2 of DKK1 is required and sufficient for binding to KRM1: In surface plasmon resonance (SPR), we measured low micromolar affinity between full-length DKK1 and immobilized KRM1ECD (Figure 2B).	RESULTS
2	13	SUMO fusion	experimental_method	A SUMO fusion of DKK1L-CRD2 displayed a similar (slightly higher) affinity.	RESULTS
17	27	DKK1L-CRD2	structure_element	A SUMO fusion of DKK1L-CRD2 displayed a similar (slightly higher) affinity.	RESULTS
66	74	affinity	evidence	A SUMO fusion of DKK1L-CRD2 displayed a similar (slightly higher) affinity.	RESULTS
15	26	SUMO fusion	experimental_method	In contrast, a SUMO fusion of DKK1CRD1-L did not display binding for concentrations tested up to 325 μM (Figure 2B).	RESULTS
30	40	DKK1CRD1-L	structure_element	In contrast, a SUMO fusion of DKK1CRD1-L did not display binding for concentrations tested up to 325 μM (Figure 2B).	RESULTS
13	32	DKK1-KRM1 interface	site	Overall, the DKK1-KRM1 interface is characterized by a large number of polar interactions but only few hydrophobic contacts (Figure 2C).	RESULTS
71	89	polar interactions	bond_interaction	Overall, the DKK1-KRM1 interface is characterized by a large number of polar interactions but only few hydrophobic contacts (Figure 2C).	RESULTS
103	123	hydrophobic contacts	bond_interaction	Overall, the DKK1-KRM1 interface is characterized by a large number of polar interactions but only few hydrophobic contacts (Figure 2C).	RESULTS
4	21	crystal structure	evidence	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
47	51	DKK1	protein	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
101	105	R191	residue_name_number	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
109	113	DKK1	protein	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
129	140	salt bridge	bond_interaction	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
144	148	D125	residue_name_number	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
153	157	E162	residue_name_number	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
161	165	KRM1	protein	The crystal structure gives an explanation for DKK1 loss-of-binding mutations identified previously: R191 of DKK1 forms a double salt bridge to D125 and E162 of KRM1 (Figure 2C).	RESULTS
2	17	charge reversal	experimental_method	A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding.	RESULTS
28	33	mouse	taxonomy_domain	A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding.	RESULTS
34	38	Dkk1	protein	A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding.	RESULTS
40	45	mDkk1	protein	A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding.	RESULTS
47	52	R197E	mutant	A charge reversal as in the mouse Dkk1 (mDkk1) R197E variant would severely disrupt the binding.	RESULTS
15	19	K226	residue_name_number	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
34	38	DKK1	protein	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
64	82	hydrophobic pocket	site	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
101	105	KRM1	protein	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
116	120	Y108	residue_name_number	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
122	125	W94	residue_name_number	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
131	135	W106	residue_name_number	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
143	155	salt bridges	bond_interaction	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
180	184	KRM1	protein	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
185	188	D88	residue_name_number	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
193	196	D90	residue_name_number	Similarly, the K226 side chain of DKK1, which points to a small hydrophobic pocket on the surface of KRM1 formed by Y108, W94, and W106, forms salt bridges with the side chains of KRM1 D88 and D90.	RESULTS
9	24	charge reversal	experimental_method	Again, a charge reversal as shown before for mDkk1 K232E would be incompatible with binding.	RESULTS
45	50	mDkk1	protein	Again, a charge reversal as shown before for mDkk1 K232E would be incompatible with binding.	RESULTS
51	56	K232E	mutant	Again, a charge reversal as shown before for mDkk1 K232E would be incompatible with binding.	RESULTS
18	22	DKK1	protein	The side chain of DKK1 S192 was also predicted to be involved in Krm binding.	RESULTS
23	27	S192	residue_name_number	The side chain of DKK1 S192 was also predicted to be involved in Krm binding.	RESULTS
65	68	Krm	protein_type	The side chain of DKK1 S192 was also predicted to be involved in Krm binding.	RESULTS
52	56	D201	residue_name_number	Indeed, we found (Figure 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198).	RESULTS
60	64	KRM1	protein	Indeed, we found (Figure 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198).	RESULTS
75	89	hydrogen bonds	bond_interaction	Indeed, we found (Figure 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198).	RESULTS
143	147	S192	residue_name_number	Indeed, we found (Figure 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198).	RESULTS
149	154	mouse	taxonomy_domain	Indeed, we found (Figure 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198).	RESULTS
156	160	S198	residue_name_number	Indeed, we found (Figure 2C) that the side chain of D201 of KRM1 forms two hydrogen bonds to the side-chain hydroxyl and the backbone amide of S192 (mouse, S198).	RESULTS
11	29	polar interactions	bond_interaction	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
53	57	N140	residue_name_number	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
59	63	S163	residue_name_number	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
69	73	Y165	residue_name_number	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
89	93	KRM1	protein	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
98	102	DKK1	protein	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
125	129	W206	residue_name_number	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
131	135	L190	residue_name_number	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
141	145	C189	residue_name_number	Additional polar interactions are formed between the N140, S163, and Y165 side chains of KRM1 and DKK1 backbone carbonyls of W206, L190, and C189, respectively.	RESULTS
16	20	DKK1	protein	The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1.	RESULTS
21	25	R224	residue_name_number	The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1.	RESULTS
29	44	hydrogen bonded	bond_interaction	The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1.	RESULTS
48	52	Y105	residue_name_number	The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1.	RESULTS
57	61	W106	residue_name_number	The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1.	RESULTS
65	69	KRM1	protein	The carbonyl of DKK1 R224 is hydrogen bonded to Y105 and W106 of KRM1.	RESULTS
20	23	Dkk	protein_type	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
24	49	charge reversal mutations	experimental_method	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
67	73	murine	taxonomy_domain	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
107	110	Krm	protein_type	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
119	124	K211E	mutant	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
129	134	R203E	mutant	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
136	141	mouse	taxonomy_domain	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
142	147	K217E	mutant	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
152	157	R209E	mutant	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
204	207	Dkk	protein_type	We suspect that the Dkk charge reversal mutations performed in the murine background and shown to diminish Krm binding K211E and R203E (mouse K217E and R209E) do so likely indirectly by disruption of the Dkk fold.	RESULTS
25	42	DKK1 binding site	site	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
46	50	KRM1	protein	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
54	65	introducing	experimental_method	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
66	85	glycosylation sites	site	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
93	95	KR	structure_element	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
97	108	90DVS92→NVS	mutant	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
114	117	WSC	structure_element	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
119	132	189VCF191→NCS	mutant	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
158	161	DKK	protein	We further validated the DKK1 binding site on KRM1 by introducing glycosylation sites at the KR (90DVS92→NVS) and WSC (189VCF191→NCS) domains pointing toward DKK (Figures 2A and 2D).	RESULTS
16	32	N-linked glycans	ptm	Introduction of N-linked glycans in protein-protein-binding sites is an established way of disrupting protein-binding interfaces.	RESULTS
36	65	protein-protein-binding sites	site	Introduction of N-linked glycans in protein-protein-binding sites is an established way of disrupting protein-binding interfaces.	RESULTS
102	128	protein-binding interfaces	site	Introduction of N-linked glycans in protein-protein-binding sites is an established way of disrupting protein-binding interfaces.	RESULTS
5	15	ectodomain	structure_element	Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte.	RESULTS
16	23	mutants	protein_state	Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte.	RESULTS
58	67	wild-type	protein_state	Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte.	RESULTS
145	148	SPR	experimental_method	Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte.	RESULTS
155	166	full-length	protein_state	Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte.	RESULTS
167	171	DKK1	protein	Both ectodomain mutants were secreted comparably with the wild-type, indicating correct folding, but failed to achieve any detectable binding in SPR using full-length DKK1 as analyte.	RESULTS
15	21	mutant	protein_state	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
45	53	N-glycan	ptm	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
66	75	interface	site	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
83	86	CUB	structure_element	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
95	108	309NQA311→NQS	mutant	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
115	124	wild-type	protein_state	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
133	137	DKK1	protein	In contrast, a mutant carrying an additional N-glycan outside the interface at the CUB domain (309NQA311→NQS), was wild-type-like in DKK1 binding (Figure 2D).	RESULTS
27	49	LRP6-KRM1 Binding Site	site	Identification of a Direct LRP6-KRM1 Binding Site	RESULTS
4	31	LRP6PE3PE4-DKK1CRD2-KRM1ECD	complex_assembly	The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6.	RESULTS
40	49	structure	evidence	The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6.	RESULTS
89	93	KRM1	protein	The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6.	RESULTS
98	102	LRP6	protein	The LRP6PE3PE4-DKK1CRD2-KRM1ECD complex structure reveals no direct interactions between KRM1 and LRP6.	RESULTS
35	47	complex with	protein_state	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
59	70	full-length	protein_state	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
71	75	LRP6	protein	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
76	86	ectodomain	structure_element	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
88	100	PE1PE2PE3PE4	structure_element	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
101	111	horse shoe	structure_element	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
155	174	electron microscopy	experimental_method	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
176	178	EM	experimental_method	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
183	211	small-angle X-ray scattering	experimental_method	We constructed in silico a ternary complex with a close to full-length LRP6 ectodomain (PE1PE2PE3PE4 horse shoe) similar to but without refinement against electron microscopy (EM) or small-angle X-ray scattering data.	RESULTS
13	19	PE3PE4	structure_element	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
33	45	superimposed	experimental_method	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
50	53	PE4	structure_element	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
59	62	PE3	structure_element	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
70	87	crystal structure	evidence	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
97	101	LRP6	protein	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
101	107	PE1PE2	structure_element	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
108	117	structure	evidence	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
122	134	superimposed	experimental_method	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
139	142	PE2	structure_element	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
148	151	PE3	structure_element	An auxiliary PE3PE4 fragment was superimposed via PE4 onto PE3 of the crystal structure, and the LRP6PE1PE2 structure was superimposed via PE2 onto PE3 of this auxiliary fragment (Figure 3A).	RESULTS
98	117	Ca2+-binding region	site	For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 β propeller of LRP6.	RESULTS
121	125	KRM1	protein	For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 β propeller of LRP6.	RESULTS
150	153	PE2	structure_element	For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 β propeller of LRP6.	RESULTS
154	165	β propeller	structure_element	For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 β propeller of LRP6.	RESULTS
169	173	LRP6	protein	For this crude approximation of a true ternary complex, we noted very close proximity between the Ca2+-binding region of KRM1 and the top face of the PE2 β propeller of LRP6.	RESULTS
4	19	solvent-exposed	protein_state	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
29	33	R307	residue_name_number	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
35	39	I308	residue_name_number	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
45	49	N309	residue_name_number	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
65	95	Ca2+-binding β connection loop	structure_element	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
99	103	KRM1	protein	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
193	205	binding site	site	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
209	221	β propellers	structure_element	The solvent-exposed residues R307, I308, and N309 of the central Ca2+-binding β connection loop of KRM1 would be almost ideally positioned for binding to this face, which is commonly used as a binding site on β propellers.	RESULTS
20	28	arginine	residue_name	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
29	35	lysine	residue_name	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
37	47	isoleucine	residue_name	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
53	63	asparagine	residue_name	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
84	97	N-X-I-(G)-R/K	structure_element	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
120	124	DKK1	protein	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
129	133	SOST	protein	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
145	149	LRP6	protein	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
161	172	propeller 1	structure_element	Peptides containing arginine/lysine, isoleucine, and asparagine (consensus sequence N-X-I-(G)-R/K) are also employed by DKK1 and SOST to bind to LRP6 (albeit to propeller 1; Figure 3B).	RESULTS
31	35	KRM1	protein	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
35	38	CUB	structure_element	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
39	47	binds to	protein_state	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
48	52	LRP6	protein	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
52	55	PE2	structure_element	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
65	68	SPR	experimental_method	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
97	106	wild-type	protein_state	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
115	130	GlycoCUB mutant	protein_state	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
134	138	KRM1	protein	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
138	141	ECD	structure_element	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
154	174	N-glycosylation site	site	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
178	182	N309	residue_name_number	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
200	204	LRP6	protein	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
204	210	PE1PE2	structure_element	To support the hypothesis that KRM1CUB binds to LRP6PE2, we used SPR and compared binding of the wild-type and the GlycoCUB mutant of KRM1ECD (bearing an N-glycosylation site at N309) with a purified LRP6PE1PE2 fragment.	RESULTS
29	39	absence of	protein_state	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
40	43	Dkk	protein_type	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
45	49	KRM1	protein	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
49	52	ECD	structure_element	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
53	58	bound	protein_state	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
86	88	to	protein_state	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
89	93	LRP6	protein	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
93	99	PE1PE2	structure_element	Indeed, we found that in the absence of Dkk, KRM1ECD bound with considerable affinity to LRP6PE1PE2 (Figure 3C).	RESULTS
55	59	KRM1	protein	In contrast, no saturable binding was observed between KRM1 and LRP6PE3PE4.	RESULTS
64	68	LRP6	protein	In contrast, no saturable binding was observed between KRM1 and LRP6PE3PE4.	RESULTS
68	74	PE3PE4	structure_element	In contrast, no saturable binding was observed between KRM1 and LRP6PE3PE4.	RESULTS
0	15	Introduction of	experimental_method	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
19	39	N-glycosylation site	site	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
43	47	N309	residue_name_number	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
51	55	KRM1	protein	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
55	58	ECD	structure_element	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
69	73	LRP6	protein	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
73	79	PE1PE2	structure_element	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
118	122	DKK1	protein	Introduction of an N-glycosylation site at N309 in KRM1ECD abolished LRP6PE1PE2 binding (Figure 3C), while binding to DKK1 was unaffected (Figure 2D).	RESULTS
31	43	binding site	site	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
52	56	KRM1	protein	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
56	59	CUB	structure_element	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
64	68	LRP6	protein	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
68	71	PE2	structure_element	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
119	127	Lrp6-Krm	complex_assembly	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
170	173	Wnt	protein_type	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
204	208	Lrp6	protein	We conclude that the predicted binding site between KRM1CUB and LRP6PE2 is a strong candidate for mediating the direct Lrp6-Krm interaction, which is thought to increase Wnt responsiveness by stabilizing Lrp6 at the cell surface.	RESULTS
55	67	binding site	site	Further experiments are required to pinpoint the exact binding site.	RESULTS
9	13	LRP6	protein	Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex.	RESULTS
13	16	PE1	structure_element	Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex.	RESULTS
108	124	Krm binding site	site	Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex.	RESULTS
152	160	LRP6-Krm	complex_assembly	Although LRP6PE1 appears somewhat out of reach in the modeled ternary complex, it cannot be excluded as the Krm binding site in the ternary complex and LRP6-Krm binary complex.	RESULTS
4	15	presence of	protein_state	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
16	19	DKK	protein	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
37	46	propeller	structure_element	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
48	51	PE1	structure_element	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
59	62	PE2	structure_element	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
67	71	LRP6	protein	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
89	92	Krm	protein_type	The presence of DKK may govern which propeller (PE1 versus PE2) of LRP6 is available for Krm binding.	RESULTS
37	62	KRM1CUB-LRP6PE2 interface	site	Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (Figure 3D).	RESULTS
93	96	Krm	protein_type	Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (Figure 3D).	RESULTS
121	125	LRP6	protein	Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (Figure 3D).	RESULTS
125	128	PE3	structure_element	Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (Figure 3D).	RESULTS
133	137	DKK1	protein	Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (Figure 3D).	RESULTS
137	141	CRD2	structure_element	Apparent binding across the proposed KRM1CUB-LRP6PE2 interface is expected to be higher once Krm is also cross-linked to LRP6PE3 via DKK1CRD2 (Figure 3D).	RESULTS
15	32	negative-stain EM	experimental_method	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
37	65	small-angle X-ray scattering	experimental_method	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
77	81	LRP6	protein	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
81	93	PE1PE2PE3PE4	structure_element	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
95	107	in isolation	protein_state	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
112	127	in complex with	protein_state	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
128	132	Dkk1	protein_type	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
139	156	negative-stain EM	experimental_method	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
160	171	full-length	protein_state	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
172	176	LRP6	protein	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
177	187	ectodomain	structure_element	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
204	210	curved	protein_state	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
212	225	platform-like	protein_state	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
279	282	PE2	structure_element	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
287	290	PE3	structure_element	Low-resolution negative-stain EM and small-angle X-ray scattering studies of LRP6PE1PE2PE3PE4, in isolation and in complex with Dkk1, plus negative-stain EM of full-length LRP6 ectodomain, have indicated curved, platform-like conformations but also potential flexibility between PE2 and PE3.	RESULTS
47	50	Krm	protein_type	It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences; however, such ideas await investigation.	RESULTS
55	58	Dkk	protein_type	It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences; however, such ideas await investigation.	RESULTS
90	94	LRP6	protein	It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences; however, such ideas await investigation.	RESULTS
95	105	ectodomain	structure_element	It is therefore possible that the interplay of Krm and Dkk binding can promote changes in LRP6 ectodomain conformation with functional consequences; however, such ideas await investigation.	RESULTS
20	54	structural and biophysical studies	experimental_method	Taken together, the structural and biophysical studies we report here extend our mechanistic understanding of Wnt signal regulation.	RESULTS
110	113	Wnt	protein_type	Taken together, the structural and biophysical studies we report here extend our mechanistic understanding of Wnt signal regulation.	RESULTS
16	26	ectodomain	structure_element	We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation.	RESULTS
27	36	structure	evidence	We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation.	RESULTS
49	52	Wnt	protein_type	We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation.	RESULTS
63	67	Krm1	protein_type	We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation.	RESULTS
163	167	KRM1	protein	We describe the ectodomain structure of the dual Wnt regulator Krm1, providing an explanation for the detrimental effect on health and development of a homozygous KRM1 mutation.	RESULTS
39	46	Krm-Dkk	complex_assembly	We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm.	RESULTS
101	107	Lrp5/6	protein_type	We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm.	RESULTS
109	112	Dkk	protein_type	We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm.	RESULTS
118	121	Krm	protein_type	We also reveal the interaction mode of Krm-Dkk and the architecture of the ternary complex formed by Lrp5/6, Dkk, and Krm.	RESULTS
25	42	crystal structure	evidence	Furthermore, the ternary crystal structure has guided in silico and biophysical analyses to suggest a direct LRP6-KRM1 interaction site.	RESULTS
54	88	in silico and biophysical analyses	experimental_method	Furthermore, the ternary crystal structure has guided in silico and biophysical analyses to suggest a direct LRP6-KRM1 interaction site.	RESULTS
109	135	LRP6-KRM1 interaction site	site	Furthermore, the ternary crystal structure has guided in silico and biophysical analyses to suggest a direct LRP6-KRM1 interaction site.	RESULTS
136	139	Krm	protein_type	Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface.	RESULTS
155	165	absence of	protein_state	Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface.	RESULTS
166	169	Dkk	protein_type	Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface.	RESULTS
185	188	Wnt	protein_type	Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface.	RESULTS
189	200	co-receptor	protein_type	Our findings provide a solid foundation for additional studies to probe how ternary complex formation triggers internalization, whereas Krm binding in the absence of Dkk stabilizes the Wnt co-receptor at the cell surface.	RESULTS
0	9	Structure	evidence	Structure of Unliganded KRM1ECD	FIG
13	23	Unliganded	protein_state	Structure of Unliganded KRM1ECD	FIG
24	28	KRM1	protein	Structure of Unliganded KRM1ECD	FIG
28	31	ECD	structure_element	Structure of Unliganded KRM1ECD	FIG
8	12	KRM1	protein	(A) The KRM1ECD fold (crystal form I) colored blue to red from the N to C terminus.	FIG
12	15	ECD	structure_element	(A) The KRM1ECD fold (crystal form I) colored blue to red from the N to C terminus.	FIG
22	36	crystal form I	evidence	(A) The KRM1ECD fold (crystal form I) colored blue to red from the N to C terminus.	FIG
0	9	Cysteines	residue_name	Cysteines as ball and sticks, glycosylation sites as sticks.	FIG
30	49	glycosylation sites	site	Cysteines as ball and sticks, glycosylation sites as sticks.	FIG
10	17	calcium	chemical	The bound calcium is shown as a gray sphere.	FIG
16	21	F207S	mutant	The site of the F207S mutation associated with ectodermal dysplasia in humans is shown as mesh.	FIG
71	77	humans	species	The site of the F207S mutation associated with ectodermal dysplasia in humans is shown as mesh.	FIG
4	17	Superposition	experimental_method	(B) Superposition of the three KRM1ECD subdomains (solid) with their next structurally characterized homologs (half transparent).	FIG
31	35	KRM1	protein	(B) Superposition of the three KRM1ECD subdomains (solid) with their next structurally characterized homologs (half transparent).	FIG
35	38	ECD	structure_element	(B) Superposition of the three KRM1ECD subdomains (solid) with their next structurally characterized homologs (half transparent).	FIG
4	17	Superposition	experimental_method	(C) Superposition of KRM1ECD from the three crystal forms.	FIG
21	25	KRM1	protein	(C) Superposition of KRM1ECD from the three crystal forms.	FIG
25	28	ECD	structure_element	(C) Superposition of KRM1ECD from the three crystal forms.	FIG
44	57	crystal forms	evidence	(C) Superposition of KRM1ECD from the three crystal forms.	FIG
0	16	Alignment scores	evidence	Alignment scores for each pairing are indicated on the dashed triangle.	FIG
8	17	structure	evidence	(A) The structure of the ternary LRP6PE3PE4-DKK1CRD2-KRM1ECD complex.	FIG
33	60	LRP6PE3PE4-DKK1CRD2-KRM1ECD	complex_assembly	(A) The structure of the ternary LRP6PE3PE4-DKK1CRD2-KRM1ECD complex.	FIG
0	4	DKK1	protein	DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green).	FIG
40	43	PE3	structure_element	DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green).	FIG
54	58	LRP6	protein	DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green).	FIG
74	80	KR-WSC	structure_element	DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green).	FIG
96	100	KRM1	protein	DKK1 (orange) is sandwiched between the PE3 module of LRP6 (blue) and the KR-WSC domain pair of KRM1 (green).	FIG
36	61	N-glycan attachment sites	site	Colored symbols indicate introduced N-glycan attachment sites (see D).	FIG
4	7	SPR	experimental_method	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
34	45	full-length	protein_state	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
46	50	DKK1	protein	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
55	67	SUMO fusions	experimental_method	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
71	75	DKK1	protein	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
115	124	wild-type	protein_state	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
125	129	KRM1	protein	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
129	132	ECD	structure_element	(B) SPR data comparing binding of full-length DKK1 and SUMO fusions of DKK1 truncations for binding to immobilized wild-type KRM1ECD.	FIG
25	51	DKK1CRD2-KRM1ECD interface	site	(C) Close-up view of the DKK1CRD2-KRM1ECD interface.	FIG
21	30	interface	site	Residues involved in interface formation are shown as sticks; those mentioned in the text are labeled.	FIG
0	12	Salt bridges	bond_interaction	Salt bridges are in pink and hydrogen bonds in black.	FIG
29	43	hydrogen bonds	bond_interaction	Salt bridges are in pink and hydrogen bonds in black.	FIG
4	7	SPR	experimental_method	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
8	20	binding data	evidence	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
31	35	DKK1	protein	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
57	66	wild-type	protein_state	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
67	71	KRM1	protein	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
71	74	ECD	structure_element	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
102	112	engineered	protein_state	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
113	132	glycosylation sites	site	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
140	142	KR	structure_element	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
147	150	WSC	structure_element	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
187	191	DKK1	protein	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
204	207	CUB	structure_element	(D) SPR binding data comparing DKK1 analyte binding with wild-type KRM1ECD and three variants bearing engineered glycosylation sites on the KR and WSC domains (green and blue pointing to DKK1) and on the CUB domain (orange).	FIG
0	9	LRP6-KRM1	complex_assembly	LRP6-KRM1 Direct Interaction and Summary	FIG
35	47	complex with	protein_state	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
57	69	β propellers	structure_element	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
73	77	LRP6	protein	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
78	84	intact	protein_state	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
90	93	CUB	structure_element	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
116	135	Ca2+-binding region	site	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
163	181	second β propeller	structure_element	(A) In a construction of a ternary complex with all four β propellers of LRP6 intact, the CUB domain points via its Ca2+-binding region toward the top face of the second β propeller.	FIG
35	51	interaction site	site	(B) Close-up view of the potential interaction site.	FIG
13	17	LRP6	protein	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
17	20	PE2	structure_element	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
30	42	superimposed	experimental_method	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
48	52	DKK1	protein	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
66	70	SOST	protein	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
99	103	LRP6	protein	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
103	106	PE1	structure_element	In addition, LRP6PE2 has been superimposed with DKK1 (yellow) and SOST (pink) peptide complexes of LRP6PE1.	FIG
4	20	SPR measurements	experimental_method	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
31	35	LRP6	protein	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
35	41	PE1PE2	structure_element	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
55	64	wild-type	protein_state	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
65	69	KRM1	protein	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
69	72	ECD	structure_element	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
81	96	GlycoCUB mutant	protein_state	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
108	116	N-glycan	ptm	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
120	124	N309	residue_name_number	(C) SPR measurements comparing LRP6PE1PE2 binding with wild-type KRM1ECD and the GlycoCUB mutant bearing an N-glycan at N309.	FIG
95	98	Wnt	protein_type	(D) Schematic representation of structural and biophysical findings and their implications for Wnt-dependent (left, middle) and independent (right) signaling.	FIG
48	52	LRP6	protein	Conformational differences in the depictions of LRP6 are included purely for ease of representation.	FIG
0	37	Diffraction and Refinement Statistics	evidence	Diffraction and Refinement Statistics	TABLE
1	5	KRM1	protein	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
5	8	ECD	structure_element	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
9	13	KRM1	protein	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
13	16	ECD	structure_element	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
17	21	KRM1	protein	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
21	24	ECD	structure_element	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
25	29	KRM1	protein	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
29	32	ECD	structure_element	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
33	59	LRP6PE3PE4-DKKCRD2-KRM1ECD	complex_assembly	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
1295	1300	Water	chemical	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
1417	1422	Water	chemical	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
1466	1470	RMSD	evidence	"	KRM1ECD	KRM1ECD	KRM1ECD	KRM1ECD	LRP6PE3PE4-DKKCRD2-KRM1ECD	 	Crystal form	I	I	II	III	I	 	X-ray source	Diamond i04	Diamond i03	Diamond i03	Diamond i04	Diamond i04	 	Wavelength (Å)	0.9793	0.9700	0.9700	0.9795	0.9795	 	Space group	P3121	P3121	P43	P41212	C2221	 	Unit cell a/α (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	86.9/90	 	b/β (Å/°)	50.9/90	50.5/90	65.8/90	67.8/90	100.1/90	 	c/γ (Å/°)	188.4/120	187.4/120	75.0/90	198.2/90	270.7/90	 	Wilson B factor (Å2)	31	41	76	77	NA	 	Resolution range (Å)	47.10–1.90 (1.95–1.90)	62.47–2.10 (2.16–2.10)	75.00–2.80 (2.99–2.80)	67.80–3.20 (3.42–3.20)	67.68–3.50 (7.16–6.40, 3.92–3.50)	 	Unique reflections	23,300 (1,524)	17,089 (1,428)	7,964 (1,448)	8,171 (1,343)	8,070 (723, 645)	 	Average multiplicity	9.1 (9.2)	5.2 (5.3)	3.7 (3.7)	22.7 (12.6)	3.8 (3.5, 4.4)	 	Completeness (%)	99.8 (98.5)	100 (100)	99.8 (100)	98.8 (93.4)	51.6 (98.5, 14.1)	 	<I/σI>	11.4 (1.7)	12.0 (1.7)	14.9 (1.5)	13.1 (1.9)	4.6 (4.1, 2.2)	 	Rmerge (%)	14.8 (158.3)	9.3 (98.0)	6.2 (98.9)	29.8 (142.2)	44.9 (40.5, 114.2)	 	Rpim (%)	15.7 (55.3)	10.3 (109.0)	3.7 (53.8)	6.3 (40.0)	24.7 (23.9, 59.9)	 		 	Refinement	 		 	Rwork (%)	17.9	18.4	21.6	20.2	32.1	 	Rfree (%)	22.7	23.2	30.7	27.1	35.5	 		 	No. of Non-Hydrogen Atoms	 		 	Protein	2,260	2,301	2,102	2,305	7,730	 	N-glycans	42	42	28	28	0	 	Water	79	54	0	2	0	 	Ligands	6	6	2	5	0	 		 	Average B factor (Å2)	 		 	Protein	63	65	108	84	–	 	N-glycans	35	46	102	18	–	 	Water	68	85	–	75	–	 	Ligands	36	47	91	75	66	 		 	RMSD from Ideality	 		 	Bond lengths (Å)	0.020	0.016	0.019	0.016	0.004	 	Bond angles (°)	2.050	1.748	1.952	1.796	0.770	 		 	Ramachandran Plot	 		 	Favored (%)	96.8	95.5	96.9	94.9	92.3	 	Allowed (%)	99.7	100.0	100.0	99.7	99.8	 	Number of outliers	1	0	0	1	2	 	PDB code	5FWS	5FWT	5FWU	5FWV	5FWW	 	"	TABLE
99	115	diffraction data	evidence	An additional shell given for the ternary complex corresponds to the last shell with near-complete diffraction data.	TABLE