Constrained geometric simulation of the nicotinic acetylcholine receptor

被引：7

作者：

Belfield, William J. ^{[1
]}

Cole, Daniel J. ^{[1
,2
]}

Martin, Ian L. ^{[3
]}

Payne, Mike C. ^{[1
]}

Chau, P. -L ^{[4
]}

机构：

[1] Univ Cambridge, Dept Phys, Cavendish Lab, Condensed Matter Theory Grp, Cambridge CB3 0HE, England

[2] Yale Univ, Dept Chem, New Haven, CT 06520 USA

[3] Univ Alberta, Dept Pharmacol, Edmonton, AB, Canada

[4] Inst Pasteur, CNRS, UMR 3528, F-75724 Paris, France

来源：

JOURNAL OF MOLECULAR GRAPHICS & MODELLING | 2014年 / 52卷

基金：

英国工程与自然科学研究理事会;

关键词：

Nicotinic acetylcholine receptor; FRODA; FIRST; Membrane protein; Cys-loop receptors; Ligand-gated ion channels; INTRACELLULAR DOMAIN; MOLECULAR-DYNAMICS; GATING MECHANISM; FLEXIBILITY; MOTION;

D O I：

10.1016/j.jmgm.2014.05.001

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Constrained geometric simulations have been performed for the recently published closed-channel state of the nicotinic acetylcholine receptor. These simulations support the theory that correlated motion in the flexible beta-sheet structure of the extracellular domain helps to communicate a "conformational wave", spreading from the acetylcholine binding pocket. Furthermore, we have identified key residues that act at the interface between subunits and between domains that could potentially facilitate rapid communication between the binding site and the transmembrane gate. (C) 2014 Published by Elsevier Inc.

引用

页码：1 / 10

页数：10

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