1rlw: Difference between revisions

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-[[Image:1rlw.gif|left|200px]]<br />
-<applet load="1rlw" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1rlw, resolution 2.4&Aring;" />
-'''CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2'''<br />
-==Overview==
+==CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2==
-Cytosolic phospholipase A2 (cPLA2) is a calcium-sensitive 85-kDa enzyme, that hydrolyzes arachidonic acid-containing membrane phospholipids to, initiate the biosynthesis of eicosanoids and platelet-activating factor, potent inflammatory mediators. The calcium-dependent activation of the, enzyme is mediated by an N-terminal C2 domain, which is responsible for, calcium-dependent translocation of the enzyme to membranes and that, enables the intact enzyme to hydrolyze membrane-resident substrates. The, 2.4-A x-ray crystal structure of this C2 domain was solved by multiple, isomorphous replacement and reveals a beta-sandwich with the same topology, as the C2 domain from phosphoinositide-specific phospholipase C delta 1., Two clusters of exposed hydrophobic residues surround two adjacent ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9430701 (full description)]]
+<StructureSection load='1rlw' size='340' side='right'caption='[[1rlw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1rlw]] 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=1RLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RLW FirstGlance]. <br>
+</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>
+<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=CD:CADMIUM+ION'>CD</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rlw OCA], [https://pdbe.org/1rlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rlw RCSB], [https://www.ebi.ac.uk/pdbsum/1rlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rlw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== 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/rl/1rlw_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=1rlw ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-RLW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CD and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: CA1, CA2, CR1, CR2 and CR3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RLW OCA]].
+*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9430701 9430701]
 [[Category: Homo sapiens]]
-[[Category: Phospholipase A(2)]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Perisic O]]
-[[Category: Perisic, O.]]
+[[Category: Williams RL]]
-[[Category: Williams, R.L.]]
-[[Category: CA]]
-[[Category: CD]]
-[[Category: c2 domain]]
-[[Category: calb domain]]
-[[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:03:30 2007''