2i0u
From Proteopedia
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| - | [[Image:2i0u.jpg|left|200px]]<br /><applet load="2i0u" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2i0u, resolution 2.2Å" /> | ||
| - | '''Crystal structures of phospholipases A2 from Vipera nikolskii venom revealing Triton X-100 bound in hydrophobic channel'''<br /> | ||
| - | == | + | ==Crystal structures of phospholipases A2 from Vipera nikolskii venom revealing Triton X-100 bound in hydrophobic channel== |
| - | + | <StructureSection load='2i0u' size='340' side='right'caption='[[2i0u]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2i0u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vipera_berus_nikolskii Vipera berus nikolskii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I0U 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]] 2.2Å</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</scene>, <scene name='pdbligand=TRT:FRAGMENT+OF+TRITON+X-100'>TRT</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=2i0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i0u OCA], [https://pdbe.org/2i0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i0u RCSB], [https://www.ebi.ac.uk/pdbsum/2i0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i0u ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | [[ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/PA2B1_VIPNI PA2B1_VIPNI] Heterodimer: shows the same activities as the monomer, but with a lower potency. Monomer: snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity, anticoagulant activity and that weakly inhibits ADP-induced platelet aggregation (PubMed:18083205). Inhibits exocytosis in pancreatic beta cells, confirming it can act presynaptically in inhibiting the exocytosis of neurotransmitters in neurons (PubMed:19500614). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18083205</ref> <ref>PMID:19500614</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/i0/2i0u_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=2i0u ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Vipera berus nikolskii]] | ||
| + | [[Category: Bi RC]] | ||
| + | [[Category: Gao W]] | ||
Current revision
Crystal structures of phospholipases A2 from Vipera nikolskii venom revealing Triton X-100 bound in hydrophobic channel
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