1cjy

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[[Image:1cjy.gif|left|200px]]
 
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{{Structure
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==HUMAN CYTOSOLIC PHOSPHOLIPASE A2==
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|PDB= 1cjy |SIZE=350|CAPTION= <scene name='initialview01'>1cjy</scene>, resolution 2.5&Aring;
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<StructureSection load='1cjy' size='340' side='right'caption='[[1cjy]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene>
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<table><tr><td colspan='2'>[[1cjy]] 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=1CJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJY FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]
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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]] 2.5&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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}}
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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=1cjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjy OCA], [https://pdbe.org/1cjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjy RCSB], [https://www.ebi.ac.uk/pdbsum/1cjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PA24A_HUMAN PA24A_HUMAN] Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
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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/cj/1cjy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1cjy 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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Cytosolic phospholipase A2 initiates the biosynthesis of prostaglandins, leukotrienes, and platelet-activating factor (PAF), mediators of the pathophysiology of asthma and arthritis. Here, we report the X-ray crystal structure of human cPLA2 at 2.5 A. cPLA2 consists of an N-terminal calcium-dependent lipid-binding/C2 domain and a catalytic unit whose topology is distinct from that of other lipases. An unusual Ser-Asp dyad located in a deep cleft at the center of a predominantly hydrophobic funnel selectively cleaves arachidonyl phospholipids. The structure reveals a flexible lid that must move to allow substrate access to the active site, thus explaining the interfacial activation of this important lipase.
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'''HUMAN CYTOSOLIC PHOSPHOLIPASE A2'''
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Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism.,Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS Cell. 1999 Apr 30;97(3):349-60. PMID:10319815<ref>PMID:10319815</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 1cjy" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Cytosolic phospholipase A2 initiates the biosynthesis of prostaglandins, leukotrienes, and platelet-activating factor (PAF), mediators of the pathophysiology of asthma and arthritis. Here, we report the X-ray crystal structure of human cPLA2 at 2.5 A. cPLA2 consists of an N-terminal calcium-dependent lipid-binding/C2 domain and a catalytic unit whose topology is distinct from that of other lipases. An unusual Ser-Asp dyad located in a deep cleft at the center of a predominantly hydrophobic funnel selectively cleaves arachidonyl phospholipids. The structure reveals a flexible lid that must move to allow substrate access to the active site, thus explaining the interfacial activation of this important lipase.
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*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1CJY 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=1CJY OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism., Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS, Cell. 1999 Apr 30;97(3):349-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10319815 10319815]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Phospholipase A(2)]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Clark JD]]
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[[Category: Clark, J D.]]
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[[Category: Dessen A]]
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[[Category: Dessen, A.]]
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[[Category: Schmidt H]]
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[[Category: Schmidt, H.]]
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[[Category: Seehra J]]
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[[Category: Seehra, J.]]
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[[Category: Somers WS]]
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[[Category: Somers, W S.]]
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[[Category: Stahl M]]
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[[Category: Stahl, M.]]
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[[Category: Tang J]]
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[[Category: Tang, J.]]
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[[Category: CA]]
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[[Category: MES]]
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[[Category: hydrolase]]
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[[Category: lipid-binding]]
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[[Category: phospholipase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:19 2008''
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Current revision

HUMAN CYTOSOLIC PHOSPHOLIPASE A2

PDB ID 1cjy

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