2gmv
From Proteopedia
Contents |
PEPCK complex with a GTP-competitive inhibitor
Template:ABSTRACT PUBMED 17532214
Disease
[PPCKC_HUMAN] Defects in PCK1 are the cause of cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:261680]. A metabolic disorder resulting from impaired gluconeogenesis. It is a rare disease with less than 10 cases reported in the literature. Clinical characteristics include hypotonia, hepatomegaly, failure to thrive, lactic acidosis and hypoglycemia. Autoposy reveals fatty infiltration of both the liver and kidneys. The disorder is transmitted as an autosomal recessive trait.
Function
[PPCKC_HUMAN] Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
About this Structure
2gmv is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Pietranico SL, Foley LH, Huby N, Yun W, Dunten P, Vermeulen J, Wang P, Toth K, Ramsey G, Gubler ML, Wertheimer SJ. C-8 Modifications of 3-alkyl-1,8-dibenzylxanthines as inhibitors of human cytosolic phosphoenolpyruvate carboxykinase. Bioorg Med Chem Lett. 2007 Jul 15;17(14):3835-9. Epub 2007 May 22. PMID:17532214 doi:http://dx.doi.org/10.1016/j.bmcl.2007.05.013
- Foley LH, Wang P, Dunten P, Ramsey G, Gubler ML, Wertheimer SJ. X-ray structures of two xanthine inhibitors bound to PEPCK and N-3 modifications of substituted 1,8-dibenzylxanthines. Bioorg Med Chem Lett. 2003 Nov 3;13(21):3871-4. PMID:14552798
- Dunten P, Belunis C, Crowther R, Hollfelder K, Kammlott U, Levin W, Michel H, Ramsey GB, Swain A, Weber D, Wertheimer SJ. Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site. J Mol Biol. 2002 Feb 15;316(2):257-64. PMID:11851336 doi:http://dx.doi.org/10.1006/jmbi.2001.5364
