1Z6Q
Glycogen phosphorylase with inhibitor in the AMP site
Summary for 1Z6Q
| Entry DOI | 10.2210/pdb1z6q/pdb |
| Related | 1Z6P |
| Descriptor | Glycogen phosphorylase, muscle form, 4-{2,4-BIS[(3-NITROBENZOYL)AMINO]PHENOXY}PHTHALIC ACID (2 entities in total) |
| Functional Keywords | glycogen metabolism; glycogen phosphorylase b; inhibition; allosteric, transferase |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 98105.78 |
| Authors | Kristiansen, M.,Andersen, B.,Iversen, L.F.,Westergaard, N. (deposition date: 2005-03-23, release date: 2005-04-12, Last modification date: 2011-07-13) |
| Primary citation | Kristiansen, M.,Andersen, B.,Iversen, L.F.,Westergaard, N. Identification, synthesis and chracterization of new glycogen phosphorylase inhibitors binding to the allosteric AMP site J.Med.Chem., 47:3537-3545, 2004 Cited by PubMed Abstract: Inhibition of glycogen phosphorylase (GP) has attracted considerable attention during the last five to 10 years as a means of treating the elevated hepatic glucose production seen in patients with type 2 diabetes. Several different GP inhibitors binding to various binding sites of the GP enzyme have been reported in the literature. In this paper we report on a novel class of compounds that have been identified as potent GP inhibitors. Their synthesis, mode of binding to the allosteric AMP site as well as in vitro data on GP inhibition are shown. The most potent inhibitor was found to be 4-[2,4-bis-(3-nitrobenzoylamino)phenoxy]phthalic acid (4j) with an IC(50) value of 74 nM. This compound together with a closely related analogue was further characterized by enzyme kinetics and in primary rat hepatocytes. PubMed: 15214781DOI: 10.1021/jm031121n PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
Download full validation report
