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Structural and functional studies of the nicotinic acetylcholine receptor by solid-state NMR

Williamson, P.T.F., Meier, B.H. and Watts, A. (2004) Structural and functional studies of the nicotinic acetylcholine receptor by solid-state NMR European Biophysics Journal, 33, (3), pp. 247-254. (doi:10.1007/s00249-003-0380-1).

Record type: Article

Abstract

Over the last seven years, solid-state NMR has been widely employed to study structural and functional aspects of the nicotinic acetylcholine receptor. These studies have provided detailed structural information relating to both the ligand binding site and the transmembrane domain of the receptor. Studies of the ligand binding domain have elucidated the nature and the orientation of the pharmacophores responsible for the binding of the agonist acetylcholine within the agonist binding site. Analyses of small transmembrane fragments derived from the nicotinic acetylcholine receptor have also revealed the secondary structure and the orientation of these transmembrane domains. These experiments have expanded our understanding of the channel's structural properties and are providing an insight into how they might be modulated by the surrounding lipid environment. In this article we review the advances in solid-state NMR applied to the nicotinic acetylcholine receptor and compare the results with recent electron diffraction and X-ray crystallographic studies.

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More information

Published date: 1 May 2004
Keywords: integral membrane proteins, magic angle sample spinning, nicotinic acetylcholine receptor, oriented samples, solid-state NMR

Identifiers

Local EPrints ID: 56523
URI: http://eprints.soton.ac.uk/id/eprint/56523
ISSN: 0175-7571
PURE UUID: 249ff25c-a4e0-4249-8f56-d292560f956f
ORCID for P.T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

Catalogue record

Date deposited: 08 Aug 2008
Last modified: 17 Jul 2017 14:30

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Contributors

Author: B.H. Meier
Author: A. Watts

University divisions

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