4Z5X
Glycogen phosphorylase in complex with gallic acid
Summary for 4Z5X
Entry DOI | 10.2210/pdb4z5x/pdb |
Related | 4YUA |
Descriptor | Glycogen phosphorylase, muscle form, 3,4,5-trihydroxybenzoic acid, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
Functional Keywords | alpha and beta protein, transferase |
Biological source | Oryctolagus cuniculus (Rabbit) |
Total number of polymer chains | 1 |
Total formula weight | 97855.66 |
Authors | Kyriakis, E.,Kantsadi, L.A.,Stravodimos, A.G.,Chatzileontiadou, S.M.D.,Leonidas, D.D. (deposition date: 2015-04-03, release date: 2015-05-13, Last modification date: 2025-04-09) |
Primary citation | Kyriakis, E.,Stravodimos, G.A.,Kantsadi, A.L.,Chatzileontiadou, D.S.,Skamnaki, V.T.,Leonidas, D.D. Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b. Febs Lett., 589:1787-1794, 2015 Cited by PubMed Abstract: We present a study on the binding of gallic acid and its dimer ellagic acid to glycogen phosphorylase (GP). Ellagic acid is a potent inhibitor with Kis of 13.4 and 7.5 μM, in contrast to gallic acid which displays Kis of 1.7 and 3.9 mM for GPb and GPa, respectively. Both compounds are competitive inhibitors with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. However, only ellagic acid functions with glucose in a strongly synergistic mode. The crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes were determined at high resolution, revealing that both ligands bind to the inhibitor binding site of the enzyme and highlight the structural basis for the significant difference in their inhibitory potency. PubMed: 25980608DOI: 10.1016/j.febslet.2015.05.013 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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