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1m51

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Revision as of 10:54, 18 October 2017

PEPCK complex with a GTP-competitive inhibitor

Structural highlights

1m51 is a 1 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
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

The analysis of the X-ray structures of two xanthine inhibitors bound to PEPCK and a comparison to the X-ray structure of GTP bound to PEPCK are reported. The SAR at N-1, N-7 and developing SAR at C-8 are consistent with information gained from the X-ray structures of compounds 1 and 2 bound to PEPCK. Representative N-3 modifications of compound 2 that led to the discovery of 3-cyclopropylmethyl and its carboxy analogue as optimal N-3 groups are presented.

X-ray structures of two xanthine inhibitors bound to PEPCK and N-3 modifications of substituted 1,8-dibenzylxanthines.,Foley LH, Wang P, Dunten P, Ramsey G, Gubler ML, Wertheimer SJ Bioorg Med Chem Lett. 2003 Nov 3;13(21):3871-4. PMID:14552798^[1]

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

References

↑ 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m51"

@@ Line 1: / Line 1: @@
 ==PEPCK complex with a GTP-competitive inhibitor==
 <StructureSection load='1m51' size='340' side='right' caption='[[1m51]], [[Resolution|resolution]] 2.25&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=1m51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m51 OCA], [http://pdbe.org/1m51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m51 RCSB], [http://www.ebi.ac.uk/pdbsum/1m51 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=1m51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m51 OCA], [http://pdbe.org/1m51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m51 RCSB], [http://www.ebi.ac.uk/pdbsum/1m51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m51 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 21: / Line 22: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m51 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 32: / Line 33: @@
 </div>
 <div class="pdbe-citations 1m51" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Phosphoenolpyruvate carboxykinase|Phosphoenolpyruvate carboxykinase]]
 == References ==
 <references/>

1m51

From Proteopedia

Revision as of 10:54, 18 October 2017

PEPCK complex with a GTP-competitive inhibitor

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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