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PubMed · 7055628

Structure and function of an acetylcholine receptor.

J Kistler·R M Stroud·M W Klymkowsky·R A Lalancette·R H Fairclough
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Abstract

Structural analysis of an acetylcholine receptor from Torpedo californica leads to a three-dimensional model in which a "monomeric" receptor is shown to contain subunits arranged around a central ionophoretic channel, which in turn traverses the entire 110 A length of the molecule. The receptor extends approximately 15 A on the cytoplasmic side, 55 A on the synaptic side of the membrane. The alpha-bungarotoxin/agonist binding site is found to be approximately 55 A from the entrance to the central gated ion channel. A hypothesis for the mechanism of AcChR is presented which takes into account the structural and kinetic data, which is testable, and which serves as a focus for future studies on the agonist-induced structure change in AcChR.

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AnimalsBungarotoxinsModels, BiologicalMolecular ConformationNeurotoxinsReceptors, CholinergicTorpedoJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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J Kistler, R M Stroud, M W Klymkowsky, R A Lalancette, R H Fairclough. 1982. Structure and function of an acetylcholine receptor.. https://doi.org/10.1016/s0006-3495(82)84685-7

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