1rgb
From Proteopedia
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| - | [[Image:1rgb.png|left|200px]] | ||
| - | + | ==Phospholipase A2 from Vipera ammodytes meridionalis== | |
| + | <StructureSection load='1rgb' size='340' side='right'caption='[[1rgb]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1rgb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vipera_ammodytes_meridionalis Vipera ammodytes meridionalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RGB 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]] 3.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ELD:(9E)-OCTADEC-9-ENAMIDE'>ELD</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=1rgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgb OCA], [https://pdbe.org/1rgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rgb RCSB], [https://www.ebi.ac.uk/pdbsum/1rgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rgb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PA2B_VIPAE PA2B_VIPAE] Heterodimer: postsynaptic neurotoxin. Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | ||
| + | == 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/rg/1rgb_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1rgb ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The inhibition of phospholipase A(2)s (PLA(2)s) is of pharmacological and therapeutic interest because these enzymes are involved in several inflammatory diseases. Elaidoylamide is a powerful inhibitor of a neurotoxic PLA(2) from the Vipera ammodytes meridionalis venom. The X-ray structure of the enzyme-inhibitor complex reveals a new mode of Asp49 PLA(2) inhibition by a fatty acid hydrocarbon chain. The structure contains two identical homodimers in the asymmetric unit. In each dimer one subunit is rotated by 180 degrees with respect to the other and the two molecules are oriented head-to-tail. One molecule of elaidoylamide is bound simultaneously to the substrate binding sites of two associated neurotoxic phospholipase A(2) molecules. The inhibitor binds symmetrically to the hydrophobic channels of the two monomers. The structure can be used to design anti-inflammatory drugs. | ||
| - | + | Asp49 phospholipase A(2)-elaidoylamide complex: a new mode of inhibition.,Georgieva DN, Rypniewski W, Gabdoulkhakov A, Genov N, Betzel C Biochem Biophys Res Commun. 2004 Jul 9;319(4):1314-21. PMID:15194511<ref>PMID:15194511</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1rgb" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Phospholipase A2|Phospholipase A2]] | + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Vipera ammodytes meridionalis]] | [[Category: Vipera ammodytes meridionalis]] | ||
| - | [[Category: Georgieva | + | [[Category: Georgieva DN]] |
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Current revision
Phospholipase A2 from Vipera ammodytes meridionalis
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