Open AccessThe nicotinic receptor ligand binding domain
Author(s) -
Sine Steven M.
Publication year - 2002
Publication title -
journal of neurobiology
Language(s) - English
Resource type - Journals
eISSN - 1097-4695
pISSN - 0022-3034
DOI - 10.1002/neu.10139
Subject(s) - ion channel , nicotinic agonist , ligand gated ion channel , nicotinic acetylcholine receptor , cys loop receptors , biology , biophysics , gating , acetylcholine receptor , neurotransmitter receptor , ligand (biochemistry) , mutagenesis , binding site , receptor , protein subunit , biochemistry , mutation , gene
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. © 2002 Wiley Periodicals, Inc. J Neurobiol 53: 431–446, 2002