Search results
Results from the WOW.Com Content Network
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 ...
Benzodiazepines function by binding to the benzodiazepine site on most, but not all, GABA A receptors. GABA A modulation by benzodiazepine site agonists is self-limiting. The channel conductance is not higher in the presence of benzodiazepine and GABA than the conductance with the presence of only high GABA concentrations.
The subset of GABA A receptors that also bind benzodiazepines are referred to as benzodiazepine receptors (BzR). The GABA A receptor is a heteromer composed of five subunits, the most common ones being two αs, two βs, and one γ (α 2 β 2 γ1). For each subunit, many subtypes exist (α 1–6, β 1–3, and γ 1–3).
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. GABA-A ...
Bretazenil has a more broad spectrum of action than traditional benzodiazepines as it has been shown to have low affinity binding to α 4 and α 6 GABA A receptors in addition to acting on α 1, α 2, α 3 and α 5 subunits which traditional benzodiazepine drugs work on.
GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA A receptor. At least 16 distinct subunits of GABA A receptors have been
Benzodiazepines bind to the GABA A receptor inducing a conformational change leading to an increased affinity to GABA. The allosteric binding site is situated in a "pocket" created by the alpha and gamma subunits. The pharmacological effects on benzodiazepines vary based on which alpha subunit of the GABA A receptor the benzodiazepine binds to.
SH-I-048A (SH-i-048A) is a benzodiazepine derivative related in structure to compounds such as flubromazepam and meclonazepam.SH-I-048A is described as a non subtype selective superagonist at the benzodiazepine site of GABA A receptors, [1] with a binding affinity of 0.77 nM at the α 1 subtype, 0.17 nM at α 2, 0.38 nM at α 3 and 0.11 nM at α 5. [2]