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The ionotropic GABA A receptor protein complex is also the molecular target of the benzodiazepine class of tranquilizer drugs. Benzodiazepines do not bind to the same receptor site on the protein complex as does the endogenous ligand GABA (whose binding site is located between α- and β-subunits), but bind to distinct benzodiazepine binding sites situated at the interface between the α- and ...
The most common GABA receptor SNPs do not correlate with deleterious health effects in many cases, but do in a few. One significant example of a deleterious mutation is the major association between several GABA receptor gene polymorphisms and schizophrenia.
[1] [2] The effects of GABA A receptor NAMs are functionally the opposite of those of GABA A receptor positive allosteric modulators (PAMs) like the benzodiazepines, barbiturates, and ethanol . [1] [2] Non-selective GABA A receptor NAMs can produce a variety of effects including convulsions, neurotoxicity, and anxiety, among others. [1] [2]
Recent research has produced several ligands which are moderately selective for GABA A receptors containing the α 5 subunit. These have proved to be useful in investigating some of the side effects of benzodiazepine and nonbenzodiazepine drugs, particularly the effects on learning and memory such as anterograde amnesia.
In pharmacology, GABA A receptor positive allosteric modulators, also known as GABAkines or GABA A receptor potentiators, [1] are positive allosteric modulator (PAM) molecules that increase the activity of the GABA A receptor protein in the vertebrate central nervous system. GABA is a major inhibitory neurotransmitter in the central nervous system.
GABRA2 is an alpha subunit that is part of GABA-A receptors, which are ligand-gated chloride channels and are activated by the major inhibitory neurotransmitter in the mammalian brain, GABA. Chloride conductance of these channels can be modulated by agents, such as benzodiazepines (psychoactive drugs) that bind to the GABA-A receptor.