Background
The γ-aminobutyric acid type A (GABAA) receptors are the major inhibitory neurotransmitter receptors of the central nervous system. Benzodiazepine (Bz)-site ligands bind at the α/γ interface and can enhance GABA-induced Cl− currents. The efficacy of certain benzodiazepines strongly depends on the type of α(1,2,3,5) subunits in the receptors. Functionally selective compounds for α2/3 can be anxiolytic without having the side effect of sedation. The molecular basis for functional selectivity is investigated in this work.