Anxiety over GABA(A) receptor structure relieved by AChBP

Trends Biochem Sci. 2002 Jun;27(6):280-7. doi: 10.1016/s0968-0004(02)02092-3.


The GABA(A) receptor is the primary mediator of inhibitory neurotransmission in the brain and is a major target for neuromodulatory drugs such as benzodiazepines, barbiturates, ethanol and anaesthetics. However, our understanding of the molecular details of this receptor has been limited by a lack of high-resolution structural information. This article presents a new model for the extracellular, ligand-binding domain of the GABA(A) receptor, that is based on the recently determined structure of a soluble acetylcholine-binding protein. The model puts existing mutational and biochemical data into a three-dimensional context, shows details of the GABA- and benzodiazepine-binding sites, and highlights the importance of other regions in allosteric conformational change. This provides a new perspective on existing data and an exciting new framework for understanding this important family of receptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Site
  • Amino Acid Sequence
  • Benzodiazepines / metabolism
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Ion Channels / chemistry
  • Ion Channels / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, GABA-A / chemistry*
  • Receptors, GABA-A / metabolism*


  • AChBP protein, Lymnaea
  • Carrier Proteins
  • Ion Channels
  • Receptors, GABA-A
  • Benzodiazepines