Molecular dynamics simulations to the bidirectional adhesion signaling pathway of integrin α V β 3

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...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2020-05, Vol.88 (5), p.679-688
Main Authors: Kulke, Martin, Langel, Walter
Format: Article
Language:English
Subjects:
1,2-Dipalmitoylphosphatidylcholine - chemistry
1,2-Dipalmitoylphosphatidylcholine - metabolism
Binding Sites
Cell Membrane - chemistry
Cell Membrane - metabolism
Crystallography, X-Ray
Extracellular Matrix - chemistry
Extracellular Matrix - metabolism
Humans
Integrin alphaVbeta3 - chemistry
Integrin alphaVbeta3 - genetics
Integrin alphaVbeta3 - metabolism
Molecular Dynamics Simulation
Principal Component Analysis
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Thermodynamics
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Summary: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.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.25849