The nicotinic receptor ligand binding domain

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160 Scopus citations

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 languageEnglish (US)
Pages (from-to)431-446
Number of pages16
JournalJournal of Neurobiology
Volume53
Issue number4
DOIs
StatePublished - Dec 1 2002

Keywords

  • Acetylcholine binding protein
  • Agonist-induced conformational change
  • Allosteric protein
  • Homology structural model
  • Ligand-gated ion channel

ASJC Scopus subject areas

  • Neuroscience(all)
  • Cellular and Molecular Neuroscience

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