3DDS
Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK261
Summary for 3DDS
| Entry DOI | 10.2210/pdb3dds/pdb |
| Related | 3DD1 3DDW |
| Descriptor | Glycogen phosphorylase, liver form, N-acetyl-beta-D-glucopyranosylamine, PHOSPHATE ION, ... (9 entities in total) |
| Functional Keywords | gp, glycogen phosphorylase, diabetes, allosteric enzyme, carbohydrate metabolism, disease mutation, glycogen metabolism, glycogen storage disease, glycosyltransferase, nucleotide-binding, phosphoprotein, pyridoxal phosphate, transferase |
| Biological source | Homo sapiens |
| Total number of polymer chains | 2 |
| Total formula weight | 197928.98 |
| Authors | Nolte, R.T. (deposition date: 2008-06-06, release date: 2009-01-27, Last modification date: 2023-08-30) |
| Primary citation | Thomson, S.A.,Banker, P.,Bickett, D.M.,Boucheron, J.A.,Carter, H.L.,Clancy, D.C.,Cooper, J.P.,Dickerson, S.H.,Garrido, D.M.,Nolte, R.T.,Peat, A.J.,Sheckler, L.R.,Sparks, S.M.,Tavares, F.X.,Wang, L.,Wang, T.Y.,Weiel, J.E. Anthranilimide based glycogen phosphorylase inhibitors for the treatment of type 2 diabetes. Part 3: X-ray crystallographic characterization, core and urea optimization and in vivo efficacy. Bioorg.Med.Chem.Lett., 19:1177-1182, 2009 Cited by PubMed Abstract: Key binding interactions of the anthranilimide based glycogen phosphorylase a (GPa) inhibitor 2 from X-ray crystallography studies are described. This series of compounds bind to the AMP site of GP. Using the binding information the core and the phenyl urea moieties were optimized. This work culminated in the identification of compounds with single nanomolar potency as well as in vivo efficacy in a diabetic model. PubMed: 19138846DOI: 10.1016/j.bmcl.2008.12.085 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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