1aok

From Proteopedia

(Difference between revisions)

Current revision

VIPOXIN COMPLEX

Structural highlights

1aok is a 2 chain structure with sequence from Vipera ammodytes meridionalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aok"

@@ Line 1: / Line 1: @@
-[[Image:1aok.gif|left|200px]]<br /><applet load="1aok" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1aok, resolution 2.0&Aring;" />
-'''VIPOXIN COMPLEX'''<br />
-==Overview==
+==VIPOXIN COMPLEX==
-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.
+<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.
-==About this Structure==
+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>
-AOK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vipera_ammodytes_meridionalis Vipera ammodytes meridionalis] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AOK OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9276469 9276469]
+</div>
-[[Category: Phospholipase A(2)]]
+<div class="pdbe-citations 1aok" style="background-color:#fffaf0;"></div>
-[[Category: Protein complex]]
-[[Category: Vipera ammodytes meridionalis]]
-[[Category: Betzel, C.]]
-[[Category: Eschenburg, S.]]
-[[Category: Perbandt, M.]]
-[[Category: Wilson, J.C.]]
-[[Category: ACT]]
-[[Category: hydrolase]]
-[[Category: phospholipase]]
-[[Category: pla2-activity]]
-[[Category: snake-venom]]
-[[Category: vipoxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:00:14 2007''
+==See Also==
+*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Vipera ammodytes meridionalis]]
+[[Category: Betzel C]]
+[[Category: Eschenburg S]]
+[[Category: Perbandt M]]
+[[Category: Wilson JC]]

1aok

From Proteopedia

Current revision

VIPOXIN COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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