Abstract
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.
Original language | English (US) |
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Pages (from-to) | 431-446 |
Number of pages | 16 |
Journal | Journal of Neurobiology |
Volume | 53 |
Issue number | 4 |
DOIs | |
State | Published - Dec 1 2002 |
Keywords
- Acetylcholine binding protein
- Agonist-induced conformational change
- Allosteric protein
- Homology structural model
- Ligand-gated ion channel
ASJC Scopus subject areas
- General Neuroscience
- Cellular and Molecular Neuroscience