Molecular pharmacology of the nicotinic acetylcholine receptor

Abstract The functional transitions of the nicotinic acetylcholine receptor are regulated by acetylcholine binding sites and noncompetitive inhibitor binding sites. Amino acid residues contributing to these sites are being located in the sequences of the receptor subunits. The relative proximity on the α-subunit of portions of the acetylcholine binding site and of a noncompetitive inhibitor site might be a structural basis for the interaction of these sites and suggests a model for channel gating. In this review, Arthur Karlin, Peter Kao and Mario DiPaolo will focus on these functional sites.