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The benzodiazepine binding site of GABAA receptors.
Journal article

The benzodiazepine binding site of GABAA receptors.

  • Sigel E Department of Pharmacology, University of Bern, Switzerland.
  • Buhr A
  • 1998-01-14
Published in:
  • Trends in pharmacological sciences. - 1997
Amino Acid Sequence
Animals
Benzodiazepines
Binding Sites
Humans
Molecular Sequence Data
Receptors, GABA-A
English The GABAA receptor belongs, along with the nicotinic acetylcholine receptor, the glycine receptor and the 5-HT3 receptor, to a family of homologous transmitter-gated ion channels mediating fast synaptic transmission. Many classes of drug interact with the GABAA receptor, which is the major inhibitory ion channel in the mammalian brain. Among these drugs are the allosteric modulators acting at the benzodiazepine binding site. In this article, Erwin Sigel and Andreas Buhr discuss recent studies that have identified amino acid residues that are thought to form the binding pocket for these compounds. These residues are probably located at subunit interfaces of the protein pentamer and at least some of them are homologous to residues implicated in channel agonist binding. This implies pseudosymmetry of channel agonist and channel modulatory sites, which may be, as recent data indicate, a general principle realized in other pseudosymmetric protein complexes.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/87244
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