2AMV

THE STRUCTURE OF GLYCOGEN PHOSPHORYLASE B WITH AN ALKYL-DIHYDROPYRIDINE-DICARBOXYLIC ACID

Replaces:  1AMV

Summary for 2AMV

• Entry DOI: 10.2210/pdb2amv/pdb
• Descriptor: PROTEIN (GLYCOGEN PHOSPHORYLASE), PYRIDOXAL-5'-PHOSPHATE, 2,3-DICARBOXY-4-(2-CHLORO-PHENYL)-1-ETHYL-5-ISOPROPOXYCARBONYL-6-METHYL-PYRIDINIUM, ... (5 entities in total)
• Functional Keywords: glycogen phosphorylase, glycogen metabolism, diabetes, inhibitors, glycosyltransferase, transferase
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 1
• Total formula weight: 98037.28

Authors

Zographos, S.E.,Oikonomakos, N.G.,Johnson, L.N. (deposition date: 1998-10-13, release date: 1998-10-21, Last modification date: 2011-07-13)

Primary citation

Zographos, S.E.,Oikonomakos, N.G.,Tsitsanou, K.E.,Leonidas, D.D.,Chrysina, E.D.,Skamnaki, V.T.,Bischoff, H.,Goldmann, S.,Watson, K.A.,Johnson, L.N.
The structure of glycogen phosphorylase b with an alkyldihydropyridine-dicarboxylic acid compound, a novel and potent inhibitor.
Structure, 5:1413-1425, 1997

PubMed Abstract: In muscle and liver, glycogen concentrations are regulated by the reciprocal activities of glycogen phosphorylase (GP) and glycogen synthase. An alkyl-dihydropyridine-dicarboxylic acid has been found to be a potent inhibitor of GP, and as such has potential to contribute to the regulation of glycogen metabolism in the non-insulin-dependent diabetes diseased state. The inhibitor has no structural similarity to the natural regulators of GP. We have carried out structural studies in order to elucidate the mechanism of inhibition.

PubMed: 9384557
DOI: 10.1016/S0969-2126(97)00292-X

Experimental method

X-RAY DIFFRACTION (2.3 Å)