Search for: [Abstract = "g site \(S1\), while the aromatic rings of the compounds reach the S2 site within the vestibule of the transporter in the outward open state. The binding mode of the inhibitors explains the differences in the activity of their isomers, as well as the selectivity toward particular transporter types. Inhibitors with a non\-amino acid structure, including novel 4\-aminobutanamide and 4\-hydroxybutanamide derivatives as well as their analogues obtained in the Department of Physicochemical Drug Analysis JU MC, bind mainly within the vestibule of GABA transporters. Fragments that may account for the slightly different arrangement of selected derivatives in particular types of GABA transporters and contribute to their varied activity were identified. In the case of GlyT\-1, competitive inhibitors are arranged coherently at the S1 and S2 sites of the transporters. In contrast, non\-competitive inhibitors are located partially on the intracellular side of the transporter in the inward open state. This binding mode is consistent with that observed in the recently released GlyT\-1 crystal structure. In the case of GlyT\-2, the currently known ligands bind at the S1 and\/or S2 site of the transporter in the outward open state. The amino acid differences between GlyT\-1 and GlyT\-2 provide a reasonable explanation for the selectivity of the particular inhibitors. A virtual screening of"]

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