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从蛋白质结构推断配体门控离子通道超家族的通道门控机制。

Mechanisms of channel gating of the ligand-gated ion channel superfamily inferred from protein structure.

作者信息

Absalom Nathan L, Lewis Trevor M, Schofield Peter R

机构信息

Neurobiology Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia.

出版信息

Exp Physiol. 2004 Mar;89(2):145-53. doi: 10.1113/expphysiol.2003.026815. Epub 2004 Feb 17.

Abstract

The nicotinic-like ligand-gated ion channel superfamily consists of a group of structurally related receptors that activate an ion channel after the binding of extracellular ligand. The recent publications of the crystal structure of an acetylcholine binding protein and a refined electron micrograph structure of the membrane-bound segment of an acetylcholine receptor have led to insights into the molecular determinants of receptor function. Although the structures confirmed much biochemical and electrophysiological data obtained about the receptors, they also provide opportunities to study further the mechanisms that allow channel activation stimulated by ligand-binding. Here we review the mechanisms of channel gating that have been elucidated by information gained from the structures of the acetylcholine binding protein and membrane-bound segment of the acetylcholine receptor.

摘要

烟碱样配体门控离子通道超家族由一组结构相关的受体组成,这些受体在细胞外配体结合后激活离子通道。乙酰胆碱结合蛋白的晶体结构以及乙酰胆碱受体膜结合片段的精细电子显微镜结构的最新发表,使人们对受体功能的分子决定因素有了深入了解。尽管这些结构证实了许多关于受体的生化和电生理数据,但它们也为进一步研究配体结合刺激通道激活的机制提供了机会。在这里,我们回顾了通过从乙酰胆碱结合蛋白和乙酰胆碱受体膜结合片段的结构中获得的信息所阐明的通道门控机制。

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