SRC2-3 binds to vitamin D receptor with high sensitivity and strong affinity.
Vitamin D receptor (VDR) is a member of the nuclear receptor superfamily and regulates the expression of target genes through ligand binding. To express the target gene, coactivator binding to the VDR/ligand complex is essential. Although there are many coactivators in living cells, precise interactions between coactivators and VDR have not been clarified. Here, we synthesized two coactivator peptides, DRIP205-2 and SRC2-3, evaluated their affinity for the ligand-binding domain (LBD) of VDR using 1α,25-dihydroxyvitamin D3, partial agonist 1, and antagonist 2 by surface plasmon resonance (SPR), and assessed their interaction modes with VDR-LBD using X-ray crystallographic analysis. This study showed that the SRC2-3 peptide is more sensitive to the ligands (agonist, partial agonist, and antagonist) and shows more intimate interactions with VDR-LBD than DRIP205-2 peptide.
['Egawa|Daichi|D|', 'Itoh|Toshimasa|T|', 'Kato|Akira|A|', 'Kataoka|Saori|S|', 'Anami|Yasuaki|Y|', 'Yamamoto|Keiko|K|']
D001665:Binding Sites D018360:Crystallography, X-Ray D004305:Dose-Response Relationship, Drug D006801:Humans D008958:Models, Molecular D015394:Molecular Structure D010455:Peptides D018167:Receptors, Calcitriol D013329:Structure-Activity Relationship D020349:Surface Plasmon Resonance
SRC2-3 Vitamin D Nuclear receptor Coactivator Surface plasmon resonance Charge clamp Consensus motif