Binding site opening by loop C shift and chloride ion-pore interaction in the GABAAreceptor model

Abstract

Molecular dynamics simulations of the shut α₁β₂γ₂GABA_Aheteropentamer receptor homology model reveal significant differences between intersubunit interfaces (ligand binding G1, G2 and non-binding) compared to homomeric receptor assemblies and possible ion interaction sites in the top part of the transmembrane domain (TMD).