Allosteric modulations of the nicotinic acetylcholine receptor.
The nicotinic acetylcholine receptor behaves as an allosteric protein with multiple, interconvertible conformations: a resting state, an open channel state and several desensitized states. A variety of pharmacological agents and physiological ligands regulate the transitions between these states when they bind to sites topographically distinct from the acetylcholine binding site. The physiological significance of this type of regulation is discussed and its potential role in the modulation of synaptic efficacy suggested.
Léna
C
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CNRS UA D1284 Neurobiologie Moléculaire, Institut Pasteur, Paris, France.
Changeux
J P
JP
D000109:Acetylcholine / Q000378:metabolism; D000494:Allosteric Regulation; D000495:Allosteric Site; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002412:Cations / Q000378:metabolism; D006728:Hormones / Q000494:pharmacology; D015640:Ion Channel Gating; D010276:Parasympatholytics / Q000494:pharmacology; D010277:Parasympathomimetics / Q000494:pharmacology; D010766:Phosphorylation; D010830:Physostigmine / Q000494:pharmacology; D011487:Protein Conformation; D051381:Rats; D011978:Receptors, Nicotinic / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism; D015398:Signal Transduction; D014101:Torpedo
D002412:Cations; D006728:Hormones; D010276:Parasympatholytics; D010277:Parasympathomimetics; D011978:Receptors, Nicotinic; D010830:Physostigmine; D000109:Acetylcholine; D002118:Calcium