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

Williamson, P.T.F., Verhoeven, A., Miller, K.W., Meier, B.H. and Watts, A. (2007) The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor Proceedings of the National Academy of Sciences, 104, (46), pp. 18031-18036. (doi:10.1073/pnas.0704785104).

Record type: Article


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 13C-labeled atoms of acetylcholine were measured. Bound acetylcholine adopts a bent conformation characterized with a quaternary ammonium-to-carbonyl distance of 5.1 Å. In this conformation, and with its orientation constrained to that previously determined by us, the acetylcholine could be docked satisfactorily in the agonist pocket of the agonist-bound, but not the agonist-free, crystal structure of a soluble acetylcholine-binding protein from Lymnaea stagnali. The quaternary ammonium group of the acetylcholine was determined to be within 3.9 Å of five aromatic residues and its acetyl group close to residues C187/188 of the principle and residue L112 of the complementary subunit. The observed >CGraphicO chemical shift is consistent with H bonding to the nicotinic acetylcholine receptor residues ?Y116 and ?T119 that are homologous to L112 in the soluble acetylcholine-binding protein

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Published date: 2007
Organisations: Biological Sciences


Local EPrints ID: 72079
ISSN: 0027-8424
PURE UUID: eccbe104-8a32-4960-889a-d80a557ba37a
ORCID for P.T.F. Williamson: ORCID iD

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Date deposited: 20 Jan 2010
Last modified: 18 Jul 2017 23:56

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Author: A. Verhoeven
Author: K.W. Miller
Author: B.H. Meier
Author: A. Watts

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