1cvu

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[[Image:1cvu.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2==
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|PDB= 1cvu |SIZE=350|CAPTION= <scene name='initialview01'>1cvu</scene>, resolution 2.4&Aring;
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<StructureSection load='1cvu' size='340' side='right'caption='[[1cvu]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACD:ARACHIDONIC+ACID'>ACD</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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<table><tr><td colspan='2'>[[1cvu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CVU FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACD:ARACHIDONIC+ACID'>ACD</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvu OCA], [https://pdbe.org/1cvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cvu RCSB], [https://www.ebi.ac.uk/pdbsum/1cvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cvu ProSAT]</span></td></tr>
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|RELATEDENTRY=[[6cox|6COX]], [[5cox|5COX]], [[1cqe|1CQE]], [[1lox|1LOX]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvu OCA], [http://www.ebi.ac.uk/pdbsum/1cvu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cvu RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PGH2_MOUSE PGH2_MOUSE] Mediates the formation of prostaglandins from arachidonate. May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity.<ref>PMID:12925531</ref> <ref>PMID:20463020</ref> <ref>PMID:20810665</ref> <ref>PMID:21489986</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cvu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1cvu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclooxygenases are bifunctional enzymes that catalyse the first committed step in the synthesis of prostaglandins, thromboxanes and other eicosanoids. The two known cyclooxygenases isoforms share a high degree of amino-acid sequence similarity, structural topology and an identical catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential reactions in spatially distinct, but mechanistically coupled active sites. The initial cyclooxygenase reaction converts arachidonic acid (which is achiral) to prostaglandin G2 (which has five chiral centres). The subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin H2. Here we report the co-crystal structures of murine apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin. These structures suggest the molecular basis for the stereospecificity of prostaglandin G2 synthesis.
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'''CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2'''
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Structural insights into the stereochemistry of the cyclooxygenase reaction.,Kiefer JR, Pawlitz JL, Moreland KT, Stegeman RA, Hood WF, Gierse JK, Stevens AM, Goodwin DC, Rowlinson SW, Marnett LJ, Stallings WC, Kurumbail RG Nature. 2000 May 4;405(6782):97-101. PMID:10811226<ref>PMID:10811226</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1cvu" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Cyclooxygenases are bifunctional enzymes that catalyse the first committed step in the synthesis of prostaglandins, thromboxanes and other eicosanoids. The two known cyclooxygenases isoforms share a high degree of amino-acid sequence similarity, structural topology and an identical catalytic mechanism. Cyclooxygenase enzymes catalyse two sequential reactions in spatially distinct, but mechanistically coupled active sites. The initial cyclooxygenase reaction converts arachidonic acid (which is achiral) to prostaglandin G2 (which has five chiral centres). The subsequent peroxidase reaction reduces prostaglandin G2 to prostaglandin H2. Here we report the co-crystal structures of murine apo-cyclooxygenase-2 in complex with arachidonic acid and prostaglandin. These structures suggest the molecular basis for the stereospecificity of prostaglandin G2 synthesis.
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*[[Cyclooxygenase 3D structures|Cyclooxygenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1CVU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVU OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structural insights into the stereochemistry of the cyclooxygenase reaction., Kiefer JR, Pawlitz JL, Moreland KT, Stegeman RA, Hood WF, Gierse JK, Stevens AM, Goodwin DC, Rowlinson SW, Marnett LJ, Stallings WC, Kurumbail RG, Nature. 2000 May 4;405(6782):97-101. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10811226 10811226]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Prostaglandin-endoperoxide synthase]]
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[[Category: Gierse JK]]
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[[Category: Single protein]]
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[[Category: Goodwin DC]]
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[[Category: Gierse, J K.]]
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[[Category: Kiefer JR]]
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[[Category: Goodwin, D C.]]
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[[Category: Kurumbail RG]]
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[[Category: Kiefer, J R.]]
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[[Category: Marnett LJ]]
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[[Category: Kurumbail, R G.]]
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[[Category: Moreland KT]]
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[[Category: Marnett, L J.]]
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[[Category: Pawlitz JL]]
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[[Category: Moreland, K T.]]
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[[Category: Rowlinson SW]]
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[[Category: Pawlitz, J L.]]
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[[Category: Stallings WC]]
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[[Category: Rowlinson, S W.]]
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[[Category: Stegeman RA]]
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[[Category: Stallings, W C.]]
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[[Category: Stevens AM]]
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[[Category: Stegeman, R A.]]
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[[Category: Stevens, A M.]]
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[[Category: arachidonate]]
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[[Category: cox-2]]
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[[Category: cyclooxygenase]]
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[[Category: endoperoxide]]
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[[Category: prostaglandin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:29:35 2008''
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Current revision

CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2

PDB ID 1cvu

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