1og2: Difference between revisions

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-[[Image:1og2.png|left|200px]]
-<!--
+==Structure of human cytochrome P450 CYP2C9==
-The line below this paragraph, containing "STRUCTURE_1og2", creates the "Structure Box" on the page.
+<StructureSection load='1og2' size='340' side='right'caption='[[1og2]], [[Resolution|resolution]] 2.60&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'>[[1og2]] is a 2 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=1OG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OG2 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]] 2.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-{{STRUCTURE_1og2|  PDB=1og2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1og2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1og2 OCA], [https://pdbe.org/1og2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1og2 RCSB], [https://www.ebi.ac.uk/pdbsum/1og2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1og2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CP2C9_HUMAN CP2C9_HUMAN] Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan.
+== 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/og/1og2_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=1og2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cytochrome P450 proteins (CYP450s) are membrane-associated haem proteins that metabolize physiologically important compounds in many species of microorganisms, plants and animals. Mammalian CYP450s recognize and metabolize diverse xenobiotics such as drug molecules, environmental compounds and pollutants. Human CYP450 proteins CYP1A2, CYP2C9, CYP2C19, CYP2D6 and CYP3A4 are the major drug-metabolizing isoforms, and contribute to the oxidative metabolism of more than 90% of the drugs in current clinical use. Polymorphic variants have also been reported for some CYP450 isoforms, which has implications for the efficacy of drugs in individuals, and for the co-administration of drugs. The molecular basis of drug recognition by human CYP450s, however, has remained elusive. Here we describe the crystal structure of a human CYP450, CYP2C9, both unliganded and in complex with the anti-coagulant drug warfarin. The structure defines unanticipated interactions between CYP2C9 and warfarin, and reveals a new binding pocket. The binding mode of warfarin suggests that CYP2C9 may undergo an allosteric mechanism during its function. The newly discovered binding pocket also suggests that CYP2C9 may simultaneously accommodate multiple ligands during its biological function, and provides a possible molecular basis for understanding complex drug-drug interactions.
-===STRUCTURE OF HUMAN CYTOCHROME P450 CYP2C9===
+Crystal structure of human cytochrome P450 2C9 with bound warfarin.,Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. PMID:12861225<ref>PMID:12861225</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12861225}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1og2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12861225 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_12861225}}
-==About this Structure==
-[[1og2]] is a 2 chain structure of [[Cytochrome P450]] with 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=1OG2 OCA].
 ==See Also==
-*[[Cytochrome P450]]
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:12861225</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Unspecific monooxygenase]]
+[[Category: Large Structures]]
-[[Category: Angove, H C.]]
+[[Category: Angove HC]]
-[[Category: Cosme, J.]]
+[[Category: Cosme J]]
-[[Category: Jhoti, H.]]
+[[Category: Jhoti H]]
-[[Category: Vinkovic, D Matak.]]
+[[Category: Matak Vinkovic D]]
-[[Category: Ward, A.]]
+[[Category: Ward A]]
-[[Category: Williams, P A.]]
+[[Category: Williams PA]]
-[[Category: Drug metabolism]]
-[[Category: Electron transport]]
-[[Category: Heme]]
-[[Category: Monooxygenase]]
-[[Category: Oxidoreductase]]