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2gmv

From Proteopedia

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Revision as of 07:18, 20 June 2018

PEPCK complex with a GTP-competitive inhibitor

Structural highlights

2gmv is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1khb, 1nhx, 1m51
Gene:	PCK1 (HUMAN)
Activity:	Phosphoenolpyruvate carboxykinase (GTP), with EC number 4.1.1.32
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[PCKGC_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

[PCKGC_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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

New modifications on the C-8 4-aminobenzyl unit of the previously reported 3-alkyl-1,8-dibenzylxanthine inhibitors of cPEPCK are presented. The most active compound reported here is the 5-chloro-1,3-dimethyl-1H-pyrazole-4-sulfonic acid amide derivative 2 with an IC(50) of 0.29+/-0.08 microM. An X-ray analysis of a heteroaromatic sulfonamide is presented showing a new pi-pi interaction.

C-8 Modifications of 3-alkyl-1,8-dibenzylxanthines as inhibitors of human cytosolic phosphoenolpyruvate carboxykinase.,Pietranico SL, Foley LH, Huby N, Yun W, Dunten P, Vermeulen J, Wang P, Toth K, Ramsey G, Gubler ML, Wertheimer SJ Bioorg Med Chem Lett. 2007 Jul 15;17(14):3835-9. Epub 2007 May 22. PMID:17532214^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gmv"

@@ Line 1: / Line 1: @@
 ==PEPCK complex with a GTP-competitive inhibitor==
 <StructureSection load='2gmv' size='340' side='right' caption='[[2gmv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PCK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(GTP) Phosphoenolpyruvate carboxykinase (GTP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.32 4.1.1.32] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmv OCA], [http://pdbe.org/2gmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gmv RCSB], [http://www.ebi.ac.uk/pdbsum/2gmv PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmv OCA], [http://pdbe.org/2gmv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gmv RCSB], [http://www.ebi.ac.uk/pdbsum/2gmv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gmv ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 17: / Line 18: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/2gmv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/2gmv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2gmv

From Proteopedia

Revision as of 07:18, 20 June 2018

PEPCK complex with a GTP-competitive inhibitor

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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