As knowledge of structure and function of GABAA-Rs increases, we find that allosteric modulation by clinically important CNS drugs can be explained by micro-domains within the receptor protein structure, which differ slightly but importantly among receptor subtypes. Modulation of GABAA-R by drugs with anxiolytic, sedative/hypnotic, anesthetic, and antiepileptic profiles continues to provide a target for current and pharmaceutical pipeline candidates. These actions involve multiple categories of drug binding sites on GABAA-R, the benzodiazepine sites and probably several other distinct sites for drugs like other anxiolytics, neurosteroids, general anesthetics, including barbiturates, etomidate, propofol, and volatile agents, and ethanol. The existence of receptor subtypes is now established, and exploitation for products with specific targets is in progress. It is expected that the NC-IUPHAR database on receptor classification and nomenclature will soon be expanded to the LGIC receptors, provided at no cost to the entire community.
