Molecular dynamics simulations to the bidirectional adhesion signaling pathway of integrin α
1,2-Dipalmitoylphosphatidylcholine
/ chemistry
Binding Sites
Cell Membrane
/ chemistry
Crystallography, X-Ray
Extracellular Matrix
/ chemistry
Humans
Integrin alphaVbeta3
/ chemistry
Molecular Dynamics Simulation
Principal Component Analysis
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Thermodynamics
dihedral principal component analysis
extracellular matrix
membrane protein
steered molecular dynamics
talin
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
10
04
2019
revised:
10
10
2019
accepted:
03
11
2019
pubmed:
7
11
2019
medline:
5
1
2021
entrez:
7
11
2019
Statut:
ppublish
Résumé
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.
Substances chimiques
Integrin alphaVbeta3
0
1,2-Dipalmitoylphosphatidylcholine
2644-64-6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
679-688Informations de copyright
© 2019 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals, Inc.
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