Molecular dynamics simulations to the bidirectional adhesion signaling pathway of integrin αV β3.
The bidirectional force transmission process of integrin through the cell membrane is still not well understood. Several possible mechanisms have been discussed in literature on the basis of experimental data, and in this study, we investigate these mechanisms by free and steered molecular dynamics simulations. For the first time, constant velocity pulling on the complete integrin molecule inside a dipalmitoyl-phosphatidylcholine membrane is conducted. From the results, the most likely mechanism for inside-out and outside-in signaling is the switchblade model with further separation of the transmembrane helices.
['Kulke|Martin|M|0000-0002-2689-2428', 'Langel|Walter|W|']
D015060:1,2-Dipalmitoylphosphatidylcholine D001665:Binding Sites D002462:Cell Membrane D018360:Crystallography, X-Ray D005109:Extracellular Matrix D006801:Humans D039302:Integrin alphaVbeta3 D056004:Molecular Dynamics Simulation D025341:Principal Component Analysis D011485:Protein Binding D000072756:Protein Conformation, alpha-Helical D000072757:Protein Conformation, beta-Strand D054730:Protein Interaction Domains and Motifs D013816:Thermodynamics
steered molecular dynamics dihedral principal component analysis extracellular matrix membrane protein talin