1jlt

From Proteopedia

(Difference between revisions)

Revision as of 14:33, 11 September 2015

Vipoxin Complex

Structural highlights

1jlt is a 2 chain structure with sequence from Vipaa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1aok
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PA2A_VIPAE] Heterodimer: postsynaptic neurotoxin.^[1] Monomer: Acidic phospholipase A2 homolog that is non-toxic.^[2] [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

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 a neurotoxic postsynaptic heterodimeric complex from the venom of Vipera ammodytes meridionalis, the most toxic snake in Europe. It consists of a basic and highly toxic phospholipase A(2) and an acidic non-toxic protein inhibitor. The two polypeptide chains have the same chain length and share 62% amino-acid identity. Vipoxin is a unique example of evolution of the catalytic and toxic phospholipase A(2) functions into inhibitory and non-toxic functions. The crystal structure of the complex has been determined by the molecular-replacement method and refined to 1.4 A resolution to an R factor of 18.2%. The complex formation decreases the accessible surface area of the two subunits by approximately 1480 A(2), which results in a reduction of toxicity and catalytic activity. The catalytic and substrate-binding sites of the vipoxin phospholipase A(2) are identical or similar to those of other group I/II enzymes. Two 2-methyl-2,4-pentanediol molecules are present in the hydrophobic channel close to the active site. The two subunits lack calcium ions. The negatively charged Asp49 of the phospholipase A(2), which participates in the Ca(2+)-binding sites of other snake-venom phospholipase A(2)s, is neutralized by the side chain of Lys69 from the inhibitor. Attempts have been made to identify the toxicity region and to explain the reduced catalytic activity and toxicity of the phospholipase A(2) subunit.

Structure of the neurotoxic complex vipoxin at 1.4 A resolution.,Banumathi S, Rajashankar KR, Notzel C, Aleksiev B, Singh TP, Genov N, Betzel C Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1552-9. Epub 2001, Oct 25. PMID:11679719^[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
↑ Banumathi S, Rajashankar KR, Notzel C, Aleksiev B, Singh TP, Genov N, Betzel C. Structure of the neurotoxic complex vipoxin at 1.4 A resolution. Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1552-9. Epub 2001, Oct 25. PMID:11679719

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/1jlt"

@@ Line 2: / Line 2: @@
 <StructureSection load='1jlt' size='340' side='right' caption='[[1jlt]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jlt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vipera_ammodytes_ammodytes Vipera ammodytes ammodytes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JLT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jlt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vipaa Vipaa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JLT FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aok|1aok]]</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='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=1jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jlt RCSB], [http://www.ebi.ac.uk/pdbsum/1jlt PDBsum]</span></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=1jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlt OCA], [http://pdbe.org/1jlt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jlt RCSB], [http://www.ebi.ac.uk/pdbsum/1jlt PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PA2I_VIPAE PA2I_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/PA21B_VIPAE PA21B_VIPAE]] Heterodimer: postsynaptic neurotoxin.<ref>PMID:23554559</ref> <ref>PMID:24678250</ref>   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.<ref>PMID:23554559</ref> <ref>PMID:24678250</ref>
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1jlt" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Vipera ammodytes ammodytes]]
+[[Category: Vipaa]]
 [[Category: Aleksiev, B]]
 [[Category: Banumathi, S]]

1jlt

From Proteopedia

Revision as of 14:33, 11 September 2015

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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