ALLOSTERIC MODULATIONS OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR

被引：173

作者：

LENA, C

CHANGEUX, JP

机构：

[1] CNRS UA D1284 'Neurobiologie Moléculaire', Institut Pasteur, 75724 Paris Cedex 15

来源：

TRENDS IN NEUROSCIENCES | 1993年 / 16卷 / 05期

关键词：

D O I：

10.1016/0166-2236(93)90150-K

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The nicotinic acetylcholine receptor behaves as an allosteric protein with multipole, interconvertible conformations: a resting state, an open channel state and several desensitized states. A variety of pharmological agents and physiological ligands regulate the transitions between these states when they bind to sites topographically distinct from the acetylcholine binding site. The physiological significance of this type of regulation is discussed and its potential role in the modulation of synaptic efficacy suggested.

引用

页码：181 / 186

页数：6

共 68 条

[61] ACTIVATION OF TORPEDO ACETYLCHOLINE-RECEPTORS EXPRESSED IN MOUSE FIBROBLASTS - SINGLE CHANNEL CURRENT KINETICS REVEAL DISTINCT AGONIST BINDING AFFINITIES [J].