Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state

被引：30

作者：

Ortells, MO ^{[1
]}

Barrantes, GE ^{[1
]}

Wood, C ^{[1
]}

Lunt, GG ^{[1
]}

Barrantes, FJ ^{[1
]}

机构：

[1] UNIV BATH, SCH BIOL & BIOCHEM, BATH BA1 7AY, AVON, ENGLAND

来源：

PROTEIN ENGINEERING | 1997年 / 10卷 / 05期

关键词：

molecular modelling; nicotinic acetylcholine receptor; pore; ion channel; structure-function relationships;

D O I：

10.1093/protein/10.5.511

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A model of the nicotinic acetylcholine receptor transmembrane region has been constructed which may represent the channel in its open-state. The positions of helices flanking the ion channel match those observed by electron microscopy and previously reported by others. Residues labelled, mutated or by other means known to have a strong influence on ion flux are each accessible from the lumen of the modelled channel. The model provides new insights into our current understanding of the ion channel structure, and suggests some novel explanations for the results of labelling and mutation studies such as those involving ion channel blockers and residue-dependent changes in ion selectivity.

引用

页码：511 / 517

页数：7

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