Allosteric modulation of neuronal nicotinic acetylcholine receptors.
The structure-function relationship of the neuronal nicotinic acetylcholine receptor is examined in the light of the allosteric concepts. Effects of site-directed mutagenesis as well as those caused by allosteric effector of the physiological and pharmacological receptor properties are discussed.
Department of Physiology, Medical Faculty, Geneva, Switzerland.
B
B
Buisson
D
D
Bertrand
D000494:Allosteric Regulation; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009474:Neurons / Q000502:physiology*; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011978:Receptors, Nicotinic; D011994:Recombinant Proteins