Benzodiazepines allosteric interactions with

I. Fitos, C. Lagercrantz, T. Larsson, M. Simonyi, I. Sjoholm, and Z. Tegyey, Stereoselective binding of 3-acetoxy-l,4-benzodiazepin-2-ones and 3-hydroxy-l,4-benzodi epin-2-ones to human serum albumin Selective allosteric interaction with warfarin enantiomers, Biodiem. Pharmacol., 35 263 (1986). 

Pharmacology Eszopiclone is a nonbenzodiazepine hypnotic. The precise mechanism of action of eszopiclone as a hypnotic is unknown, but its effect is believed to result from its interaction with gamma-aminobutyric acid (GABA)-receptor complexes at binding domains located close to or allosterically coupled to benzodiazepine receptors. 

GABAa is a protein with a pentameiic group of subunits (Fig. 4.7). Each subunit has approximately 200 amino acids. There are arormd fom hydrophobic regions which enable the receptor to possess allosteric pockets for interactions, and the hydrophobic region is also important to anchor the protein into the cell membrane. Barbiturates bind with a site different from the site of binding of benzodiazepines, which bind at the active site rather than changing the receptor conformation via an allosteric interaction. 

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