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1y38
From Proteopedia
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| - | [[Image:1y38.gif|left|200px]] | ||
| - | + | ==Crystal structure of the complex formed between phospholipase A2 dimer and glycerophosphate at 2.4 A resolution== | |
| - | + | <StructureSection load='1y38' size='340' side='right'caption='[[1y38]], [[Resolution|resolution]] 2.44Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1y38]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russelii_pulchella Daboia russelii pulchella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y38 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]] 2.44Å</td></tr> | |
| - | | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G3P:SN-GLYCEROL-3-PHOSPHATE'>G3P</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1y38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y38 OCA], [https://pdbe.org/1y38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y38 RCSB], [https://www.ebi.ac.uk/pdbsum/1y38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y38 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PA2B8_DABRR PA2B8_DABRR] Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18062812</ref> <ref>PMID:2115497</ref> <ref>PMID:8835338</ref> | ||
| + | == 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/y3/1y38_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=1y38 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: Daboia | + | </StructureSection> |
| - | [[Category: | + | [[Category: Daboia russelii pulchella]] |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: Jabeen | + | [[Category: Jabeen T]] |
| - | [[Category: Sharma | + | [[Category: Sharma S]] |
| - | [[Category: Singh | + | [[Category: Singh N]] |
| - | [[Category: Singh | + | [[Category: Singh TP]] |
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Current revision
Crystal structure of the complex formed between phospholipase A2 dimer and glycerophosphate at 2.4 A resolution
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