6YVE
Glycogen phosphorylase b in complex with pelargonidin 3-O-beta-D-glucoside
This is a non-PDB format compatible entry.
Summary for 6YVE
| Entry DOI | 10.2210/pdb6yve/pdb |
| Descriptor | Glycogen phosphorylase, muscle form, PYRIDOXAL-5'-PHOSPHATE, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | transferase |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 98182.07 |
| Authors | Drakou, C.E.,Gardeli, C.,Tsialtas, I.,Alexopoulos, S.,Mallouchos, A.,Koulas, S.,Tsagkarakou, A.,Asimakopoulos, D.,Leonidas, D.D.,Psarra, A.M.,Skamnaki, V.T. (deposition date: 2020-04-28, release date: 2020-11-18, Last modification date: 2024-01-24) |
| Primary citation | Drakou, C.E.,Gardeli, C.,Tsialtas, I.,Alexopoulos, S.,Mallouchos, A.,Koulas, S.M.,Tsagkarakou, A.S.,Asimakopoulos, D.,Leonidas, D.D.,Psarra, A.G.,Skamnaki, V.T. Affinity Crystallography Reveals Binding of Pomegranate Juice Anthocyanins at the Inhibitor Site of Glycogen Phosphorylase: The Contribution of a Sugar Moiety to Potency and Its Implications to the Binding Mode. J.Agric.Food Chem., 68:10191-10199, 2020 Cited by PubMed Abstract: Anthocyanins (ACNs) are dietary phytochemicals with an acknowledged therapeutic significance. Pomegranate juice (PJ) is a rich source of ACNs with potential applications in nutraceutical development. Glycogen phosphorylase (GP) catalyzes the first step of glycogenolysis and is a molecular target for the development of antihyperglycemics. The inhibitory potential of the ACN fraction of PJ is assessed through a combination of assays, investigation in hepatic cells, and X-ray crystallography studies. The ACN extract potently inhibits muscle and liver isoforms of GP. Affinity crystallography reveals the structural basis of inhibition through the binding of pelargonidin-3--glucoside at the GP inhibitor site. The glucopyranose moiety is revealed as a major determinant of potency as it promotes a structural binding mode different from that observed for other flavonoids. This inhibitory effect of the ACN scaffold and its binding mode at the GP inhibitor binding site may have significant implications for future structure-based drug design endeavors. PubMed: 32840370DOI: 10.1021/acs.jafc.0c04205 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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