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The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor.

Abstract:

The conformation of the neurotransmitter acetylcholine bound to the fully functional nicotinic acetylcholine receptor embedded in its native membrane environment has been characterized by using frequency-selective recoupling solid-state NMR. Six dipolar couplings among five resolved (13)C-labeled atoms of acetylcholine were measured. Bound acetylcholine adopts a bent conformation characterized with a quaternary ammonium-to-carbonyl distance of 5.1 A. In this conformation, and with its orienta...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.0704785104

Authors


Williamson, PT More by this author
Verhoeven, A More by this author
Miller, KW More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
104
Issue:
46
Pages:
18031-18036
Publication date:
2007-11-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:6ada172d-a0fc-4bc7-b551-dd6e778c7f9e
Source identifiers:
100910
Local pid:
pubs:100910

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