Autoregulation of phosphorylation of the nicotinic acetylcholine receptor

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Autoregulation of phosphorylation of the nicotinic acetylcholine receptor.

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Conformation of acetylcholine bound to the nicotinic acetylcholine receptor.

We report here the biologically active conformation of acetylcholine when bound to the high-affinity state of the receptor from Torpedo californica. The acetylcholine conformation was determined in the free and bound states by proton NMR two-dimensional nuclear Overhauser effects. In agreement with x-ray crystallographic data, acetylcholine in solution has an extended conformation with an avera...

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ژورنال

عنوان ژورنال: The Journal of Neuroscience

سال: 1994

ISSN: 0270-6474,1529-2401

DOI: 10.1523/jneurosci.14-05-03271.1994