3DDS

Crystal structure of glycogen phosphorylase complexed with an anthranilimide based inhibitor GSK261

3DDS の概要

• エントリーDOI: 10.2210/pdb3dds/pdb
• 関連するPDBエントリー: 3DD1 3DDW
• 分子名称: Glycogen phosphorylase, liver form, N-acetyl-beta-D-glucopyranosylamine, PHOSPHATE ION, ... (9 entities in total)
• 機能のキーワード: gp, glycogen phosphorylase, diabetes, allosteric enzyme, carbohydrate metabolism, disease mutation, glycogen metabolism, glycogen storage disease, glycosyltransferase, nucleotide-binding, phosphoprotein, pyridoxal phosphate, transferase
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 197928.98

構造登録者

Nolte, R.T. (登録日: 2008-06-06, 公開日: 2009-01-27, 最終更新日: 2023-08-30)

主引用文献

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

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: 19138846
DOI: 10.1016/j.bmcl.2008.12.085

実験手法

X-RAY DIFFRACTION (1.8 Å)