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[[Image:1aok.gif|left|200px]]
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{{STRUCTURE_1aok|  PDB=1aok  |  SCENE=  }}
'''VIPOXIN COMPLEX'''


==VIPOXIN COMPLEX==
<StructureSection load='1aok' size='340' side='right'caption='[[1aok]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1aok]] is a 2 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=1AOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOK 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=1aok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aok OCA], [https://pdbe.org/1aok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aok RCSB], [https://www.ebi.ac.uk/pdbsum/1aok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aok ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PA2HA_VIPAE PA2HA_VIPAE] Heterodimer: postsynaptic neurotoxin.<ref>PMID:23554559</ref>  Monomer: Acidic phospholipase A2 homolog that is non-toxic.<ref>PMID:23554559</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/ao/1aok_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=1aok ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vipoxin is the main toxic component in the venom of the Bulgarian snake Vipera ammodytes meridionalis, the most toxic snake in Europe. Vipoxin is a complex between a toxic phospholipase A2 (PLA2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequence homology (62%) between the two functionally different components. The structure shows that the formation of the complex in vipoxin is significantly different to that seen in many known structures of phospholipases and contradicts the assumptions made in earlier studies. The modulation of PLA2 activity is of great pharmacological interest, and the present structure will be a model for structure-based drug design.


==Overview==
Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.,Perbandt M, Wilson JC, Eschenburg S, Mancheva I, Aleksiev B, Genov N, Willingmann P, Weber W, Singh TP, Betzel C FEBS Lett. 1997 Aug 4;412(3):573-7. PMID:9276469<ref>PMID:9276469</ref>
Vipoxin is the main toxic component in the venom of the Bulgarian snake Vipera ammodytes meridionalis, the most toxic snake in Europe. Vipoxin is a complex between a toxic phospholipase A2 (PLA2) and a non-toxic protein inhibitor. The structure is of genetic interest due to the high degree of sequence homology (62%) between the two functionally different components. The structure shows that the formation of the complex in vipoxin is significantly different to that seen in many known structures of phospholipases and contradicts the assumptions made in earlier studies. The modulation of PLA2 activity is of great pharmacological interest, and the present structure will be a model for structure-based drug design.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1AOK is a [[Protein complex]] structure of sequences from [http://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=1AOK OCA].
</div>
<div class="pdbe-citations 1aok" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution., Perbandt M, Wilson JC, Eschenburg S, Mancheva I, Aleksiev B, Genov N, Willingmann P, Weber W, Singh TP, Betzel C, FEBS Lett. 1997 Aug 4;412(3):573-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9276469 9276469]
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vipera ammodytes meridionalis]]
[[Category: Vipera ammodytes meridionalis]]
[[Category: Betzel, C.]]
[[Category: Betzel C]]
[[Category: Eschenburg, S.]]
[[Category: Eschenburg S]]
[[Category: Perbandt, M.]]
[[Category: Perbandt M]]
[[Category: Wilson, J C.]]
[[Category: Wilson JC]]
[[Category: Hydrolase]]
[[Category: Phospholipase]]
[[Category: Pla2-activity]]
[[Category: Snake-venom]]
[[Category: Vipoxin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:31:00 2008''
Retrieved from "https://proteopedia.org/1aok"