The nicotinic receptor ligand binding domain.
The ligand binding domain (LBD) of the nicotinic acetylcholine receptor has served as a prototype for understanding molecular recognition in the family of neurotransmitter-gated ion channels. During the past fifty years, studies progressed from fundamental electrophysiological analyses of ACh-evoked ion flow, to biochemical purification of the receptor protein, pharmacological measurements of ligand binding, molecular cloning of receptor subunits, site-directed mutagenesis combined with functional analysis and recently, atomic structural determination. The emerging picture of the nicotinic receptor LBD is a specialized pocket of aromatic and hydrophobic residues formed at interfaces between protein subunits that changes conformation to convert agonist binding into gating of an intrinsic ion channel.
Sine
Steven M
SM
Department of Physiology and Biophysics, Mayo Foundation, Rochester, Minnesota 55905, USA. sine@mayo.edu
D000109:Acetylcholine / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology; D008024:Ligands; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry* / Q000378:metabolism
D008024:Ligands; D011978:Receptors, Nicotinic; D000109:Acetylcholine