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y-Aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the mammalian central nervous system. The predominant effect of GABA is the interaction with a specific receptor protein which results in an increase of the chloride ion conductance of the post-synaptic membrane to produce an inhibition of neuronal firing. In recent years, much attention has been focused on this specific receptor, the GABAA receptor, and the reasons for this are two-fold. Firstly, the pharmacology of the receptor is extremely rich and a minimum of three interacting allosteric drug binding sites are known to occur within the same receptor oligomer. These include those for the site of action of the tranquillizer drugs, the benzodiazepines, and the central nervous system depressant barbiturates. Secondly, and uniquely, opposing pharmacological actions appear to be mediated through this one receptor protein. Thus compounds which interact at the benzodiazepine site can be anxiolytic, as exemplified by the often-prescribed valium, or conversely they can have anxiogenic and convulsant properties; this phenomenon has led to the unorthodox concept of the 'inverse agonist' (Haefely & Polc, 1986). The purpose of this review is to present current views on the molecular structure of the GABAA receptor, as derived from biochemical investigations. Included also will be an exciting new development in this field, the indication that the neurotransmitter receptor proteins that are ligand-gated ion channels, that is the nicotinic acetylcholine receptor, the GABAA receptor, the glycine receptor and possibly the receptors for the excitatory amino acids, belong to a superfamily of chemically gated ion channels.

Understanding the GABAA receptor: a chemically gated ion channel