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| | <StructureSection load='1aok' size='340' side='right'caption='[[1aok]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1aok' size='340' side='right'caption='[[1aok]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1aok]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOK FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aok OCA], [http://pdbe.org/1aok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aok RCSB], [http://www.ebi.ac.uk/pdbsum/1aok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aok ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PA2A_VIPAE PA2A_VIPAE]] Heterodimer: postsynaptic neurotoxin.<ref>PMID:23554559</ref> Monomer: Acidic phospholipase A2 homolog that is non-toxic.<ref>PMID:23554559</ref> [[http://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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aok_consurf.spt"</scriptWhenChecked> | | <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/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Phospholipase A2|Phospholipase A2]] | + | *[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Large Structures]] | | [[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]]
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| Structural highlights
Function
PA2HA_VIPAE Heterodimer: postsynaptic neurotoxin.[1] Monomer: Acidic phospholipase A2 homolog that is non-toxic.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Atanasov VN, Stoykova S, Goranova Y, Mitewa M, Petrova S. Acute toxicity of vipoxin and its components: is the acidic component an "inhibitor" of PLA2 toxicity? Interdiscip Toxicol. 2012 Dec;5(4):169-72. doi: 10.2478/v10102-012-0028-z. PMID:23554559 doi:http://dx.doi.org/10.2478/v10102-012-0028-z
- ↑ Atanasov VN, Stoykova S, Goranova Y, Mitewa M, Petrova S. Acute toxicity of vipoxin and its components: is the acidic component an "inhibitor" of PLA2 toxicity? Interdiscip Toxicol. 2012 Dec;5(4):169-72. doi: 10.2478/v10102-012-0028-z. PMID:23554559 doi:http://dx.doi.org/10.2478/v10102-012-0028-z
- ↑ Perbandt M, Wilson JC, Eschenburg S, Mancheva I, Aleksiev B, Genov N, Willingmann P, Weber W, Singh TP, Betzel C. Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution. FEBS Lett. 1997 Aug 4;412(3):573-7. PMID:9276469
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