TY - CONF ID - 10442/12449 A1 - Oikonomakos, N. G. A1 - A1 - Kosmopoulou, M. N. A1 - A1 - Leonidas, D. D. A1 - A1 - Chrysina, E. D. A1 - A1 - Tiraidis, C. A1 - A1 - Bischler, N. A1 - A1 - Tsitsanou, K. E. A1 - A1 - Zographos, S. E. A1 - A1 - Kostas, I. D. A1 - A1 - Eisenbrand, G. Y1 - 2006/// T1 - Indirubin and indigo analogues as potential inhibitors of glycogenolysis: structural basis of glycogen phosphorylase inhibition T2 - Indirubin, the Red Shade of Indigo JF - International Meeting on Indirubin, the Red Shade of Indigo SN - ISBN: 2-9518029-0-0 PB - Life In Progress Editions SP - 177-+EP - UR - https://hdl.handle.net/10442/12449 N2 - Indirubin and indigo analogues were discovered as novel inhibitors of glycogen phosphorylase, a target to control hyperglycaemia in type 2 diabetes. We give a structural insight into the molecular basis of enzyme inhibition by indirubin-5-sulphonate, indirubin-3’-aminooxy-acetate, and indigo-5,5’,7,7’-tetrasulphonate. The inhibitors bind at the inhibitor site, by intercalating between the side chains of Phe285 and Tyr613. In addition, two indirubin-3’-aminooxy-acetate molecules bind at the allosteric binding site and a new sub-site in the vicinity of the allosteric site. Comparative structural analyses indicate residues in the inhibitor and the allosteric sites that can be exploited to obtain more potent inhibitors. ER -