Dynamic protein interfaces and conformational landscapes of membrane protein complexes.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
04 2020
04 2020
Historique:
received:
14
10
2019
revised:
30
12
2019
accepted:
01
01
2020
pubmed:
10
2
2020
medline:
8
6
2021
entrez:
10
2
2020
Statut:
ppublish
Résumé
Dynamic interactions between membrane proteins span a range of spatio-temporal scales and determine several cellular outcomes. Experimental methods in structure determination are able to resolve static protein-protein complexes at the membrane, but lack the resolution required for disordered, flexible domains and dynamic interactions. Computational approaches could bridge the resolution gap and help to unravel molecular details underlying these crucial interactions. Here, we review current approaches to predict dynamic membrane-protein complexes, with a focus on G protein-coupled receptors (GPCRs). Ensemble coarse-grain simulations have captured the conformational heterogeneity of several membrane receptor complexes. In conjunction, the conformational plasticity of protein interfaces especially encompassing unstructured domains is well represented by atomistic simulations. A combined integrative approach will pave the way forward to understand the molecular details of these dynamic complexes.
Identifiants
pubmed: 32036279
pii: S0959-440X(20)30001-4
doi: 10.1016/j.sbi.2020.01.001
pii:
doi:
Substances chimiques
Membrane Proteins
0
Multiprotein Complexes
0
Receptors, G-Protein-Coupled
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
191-197Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.