Structural elements involved in activation of the gamma-aminobutyric acid type A (GABAA) receptor

Biochem Soc Trans. 2004 Jun;32(Pt3):540-6. doi: 10.1042/BST0320540.

Abstract

Ligand-gated ion channels function as rapid signal transducers, converting chemical signals (in the form of neurotransmitters) into electrical signals in the postsynaptic neuron. This is achieved by the recognition of neurotransmitter at its specific-binding sites, which then triggers the opening of an ion channel ('gating'). For this to occur rapidly (< 1 ms), there must be an efficient coupling between the agonist-binding site and the gate, located more than 30 angstroms (1 angstroms = 0.1 nm) away. Whereas a great deal of progress has been made in elucidating the structure and function of both the agonist-binding site and the ion permeation pathway in ligand-gated ion channels, our knowledge of the coupling mechanism between these domains has been limited. In this review, we summarize recent studies of the agonist-binding site and the ion channel in the gamma-aminobutyric acid type A receptor, and discuss those structural elements that may mediate coupling between them. We will also consider some possible molecular mechanisms of receptor activation.

Publication types

  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Crystallography, X-Ray
  • Humans
  • Ion Channels / chemistry
  • Ions
  • Ligands
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Receptors, GABA-A / chemistry*

Substances

  • Ion Channels
  • Ions
  • Ligands
  • Receptors, GABA-A