Functional domains of GABAA receptors

Trends Pharmacol Sci. 1995 May;16(5):162-8. doi: 10.1016/s0165-6147(00)89009-4.


The transmitter-gated ion channels mediate rapid synaptic transmission, for example, at the neuromuscular junction using acetylcholine and in the CNS using primarily the amino acids glutamate and GABA. GABAA-receptor Cl- channels share sequence homology with a superfamily of these channels including nicotinic acetylcholine receptor and inhibitory glycine receptor. In this article, Geoffrey Smith and Richard Olsen discuss recent affinity labelling and site-directed mutagenesis studies on GABAA receptors that have identified amino acid residues essential for binding of agonists and allosteric modulators as well as the ion channel wall formation. The structural domains identified are consistent with results obtained with other members of the transmitter-gated ion channel superfamily and suggest that structural models for one member of the family may apply to the others as well.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Benzodiazepines / metabolism
  • GABA Agonists / metabolism
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Receptors, GABA-A / chemistry
  • Receptors, GABA-A / metabolism*
  • Receptors, Glycine / chemistry
  • Receptors, Glycine / metabolism
  • Receptors, Nicotinic / metabolism


  • GABA Agonists
  • Receptors, GABA-A
  • Receptors, Glycine
  • Receptors, Nicotinic
  • Benzodiazepines