2vgb: Difference between revisions

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-{{Seed}}
-[[Image:2vgb.png|left|200px]]
-<!--
+==HUMAN ERYTHROCYTE PYRUVATE KINASE==
-The line below this paragraph, containing "STRUCTURE_2vgb", creates the "Structure Box" on the page.
+<StructureSection load='2vgb' size='340' side='right'caption='[[2vgb]], [[Resolution|resolution]] 2.73&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'>[[2vgb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liu 1liu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGB 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]] 2.73&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
-{{STRUCTURE_2vgb|  PDB=2vgb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgb OCA], [https://pdbe.org/2vgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vgb RCSB], [https://www.ebi.ac.uk/pdbsum/2vgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vgb ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Defects in PKLR are the cause of pyruvate kinase hyperactivity (PKHYP) [MIM:[https://omim.org/entry/102900 102900]; also known as high red cell ATP syndrome. This autosomal dominant phenotype is characterized by increase of red blood cell ATP.<ref>PMID:9090535</ref>   Defects in PKLR are the cause of pyruvate kinase deficiency of red cells (PKRD) [MIM:[https://omim.org/entry/266200 266200]. A frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia.
+== Function ==
+[https://www.uniprot.org/uniprot/KPYR_HUMAN KPYR_HUMAN] Plays a key role in glycolysis (By similarity).
+== 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/vg/2vgb_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=2vgb ConSurf].
+<div style="clear:both"></div>
-===HUMAN ERYTHROCYTE PYRUVATE KINASE===
+==See Also==
+*[[Pyruvate Kinase|Pyruvate Kinase]]
+*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
-<!--
+== References ==
-The line below this paragraph, {{ABSTRACT_PUBMED_11960989}}, adds the Publication Abstract to the page
+<references/>
-(as it appears on PubMed at http://www.pubmed.gov), where 11960989 is the PubMed ID number.
+__TOC__
--->
+</StructureSection>
-{{ABSTRACT_PUBMED_11960989}}
-==About this Structure==
-VGB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liu 1liu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGB OCA].
-==Reference==
-Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia., Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A, J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11960989 11960989]
 [[Category: Homo sapiens]]
-[[Category: Pyruvate kinase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Abraham DJ]]
-[[Category: Abraham, D J.]]
+[[Category: Bianchi P]]
-[[Category: Bianchi, P.]]
+[[Category: Chiarelli L]]
-[[Category: Chiarelli, L.]]
+[[Category: Dolzan M]]
-[[Category: Dolzan, M.]]
+[[Category: Fortin R]]
-[[Category: Fortin, R.]]
+[[Category: Galizzi A]]
-[[Category: Galizzi, A.]]
+[[Category: Mattevi A]]
-[[Category: Mattevi, A.]]
+[[Category: Valentini G]]
-[[Category: Valentini, G.]]
+[[Category: Wang C]]
-[[Category: Wang, C.]]
+[[Category: Zanella A]]
-[[Category: Zanella, A.]]
-[[Category: Alternative splicing]]
-[[Category: Disease mutation]]
-[[Category: Glycolysis]]
-[[Category: Kinase]]
-[[Category: Magnesium]]
-[[Category: Metal-binding]]
-[[Category: Phosphorylation]]
-[[Category: Polymorphism]]
-[[Category: Pyruvate]]
-[[Category: Pyruvate kinase in the active r-state]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:30:28 2008''