The BZ1 receptor contains the α1 isoform.

The BZD receptor has been classified into several types, based on α subunit isoforms and clinical effects related to each type. This alteration, in turn, induces a conformational change in the GABA-A receptor's chloride channel that hyperpolarizes the cell and accounts for GABA's inhibitory effect throughout the central nervous system. BZDs bind to the pocket created by α and γ subunits and induce a conformational change in the GABA-A receptor. 3 BZDs bind to the pocket created by the α and γ subunits and induce a conformational change in the GABA-A receptor, allowing GABA to bind. 3 Isoforms 4 and 6 of the α subunit contain an arginine residue and do not have an affinity for BZDs. Within the α subunit of isoforms 1, 2, 3, and 5 resides a histidine residue (H101, H101, H126, and H105, respectively) that possesses a high affinity for BZDs. The benzodiazepine binding site is in a specific pocket at the pairing (intersection) of the α and γ subunits. Each receptor complex has 2 GABA-binding sites but only 1 BZD-binding site. GABA-A receptors contain 2 α subunits, 2 β subunits, and 1 γ subunit. The GABA-A receptor complex is composed of 5 glycoprotein subunits, each with multiple isoforms ( Figure 1). This article focuses primarily on the GABA-A receptor, with which BZDs interact. 2 The 3 GABA receptors are designated A, B, and C. GABA produces a calming effect on the brain.

GABA is inhibitory in nature and thus reduces the excitability of neurons.

GABA is the most common neurotransmitter in the central nervous system, found in high concentrations in the cortex and limbic system. The GABA-A receptor is a ligand-gated chloride-selective ion channel.

BZDs act as positive allosteric modulators on the gamma amino butyric acid (GABA)-A receptor.

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