1m51: Difference between revisions

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-[[Image:1m51.gif|left|200px]]
-<!--
+==PEPCK complex with a GTP-competitive inhibitor==
-The line below this paragraph, containing "STRUCTURE_1m51", creates the "Structure Box" on the page.
+<StructureSection load='1m51' size='340' side='right'caption='[[1m51]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1m51]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M51 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TSX:N-[4-(1-ALLYL-3-BUTYL-2,6-DIOXO-2,3,6,7-TETRAHYDRO-1H-PURIN-8-YLMETHYL)-PHENYL]-ACETAMIDE'>TSX</scene></td></tr>
-{{STRUCTURE_1m51|  PDB=1m51  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m51 OCA], [https://pdbe.org/1m51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m51 RCSB], [https://www.ebi.ac.uk/pdbsum/1m51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m51 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/PCKGC_HUMAN PCKGC_HUMAN] Defects in PCK1 are the cause of cytosolic phosphoenolpyruvate carboxykinase deficiency (C-PEPCKD) [MIM:[https://omim.org/entry/261680 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 ==
+[https://www.uniprot.org/uniprot/PCKGC_HUMAN 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/1m51_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <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/main_output.php?pdb_ID=1m51 ConSurf].
+<div style="clear:both"></div>
-'''PEPCK complex with a GTP-competitive inhibitor'''
+==See Also==
+*[[Phosphoenolpyruvate carboxykinase 3D structures|Phosphoenolpyruvate carboxykinase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
-==Disease==
-Known disease associated with this structure: Hypoglycemia due to PCK1 deficiency (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=261680 261680]]
-==About this Structure==
-M51 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M51 OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/14552798 14552798]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Dunten, P.]]
+[[Category: Dunten P]]
-[[Category: Foley, L H.]]
+[[Category: Foley LH]]
-[[Category: Wang, P.]]
+[[Category: Wang P]]
-[[Category: Wertheimer, S J.]]
+[[Category: Wertheimer SJ]]
-[[Category: Gluconeogenesis]]
-[[Category: Inhibitor]]
-[[Category: Xanthine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:38:28 2008''