1rgb

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Revision as of 15:50, 25 December 2014

Phospholipase A2 from Vipera ammodytes meridionalis

Structural highlights

1rgb is a 4 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.
Ligands:
Activity:	Phospholipase A(2), with EC number 3.1.1.4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PA21B_VIPAE] Heterodimer: postsynaptic neurotoxin.^[1] ^[2] 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.^[3] ^[4]

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

The inhibition of phospholipase A(2)s (PLA(2)s) is of pharmacological and therapeutic interest because these enzymes are involved in several inflammatory diseases. Elaidoylamide is a powerful inhibitor of a neurotoxic PLA(2) from the Vipera ammodytes meridionalis venom. The X-ray structure of the enzyme-inhibitor complex reveals a new mode of Asp49 PLA(2) inhibition by a fatty acid hydrocarbon chain. The structure contains two identical homodimers in the asymmetric unit. In each dimer one subunit is rotated by 180 degrees with respect to the other and the two molecules are oriented head-to-tail. One molecule of elaidoylamide is bound simultaneously to the substrate binding sites of two associated neurotoxic phospholipase A(2) molecules. The inhibitor binds symmetrically to the hydrophobic channels of the two monomers. The structure can be used to design anti-inflammatory drugs.

Asp49 phospholipase A(2)-elaidoylamide complex: a new mode of inhibition.,Georgieva DN, Rypniewski W, Gabdoulkhakov A, Genov N, Betzel C Biochem Biophys Res Commun. 2004 Jul 9;319(4):1314-21. PMID:15194511^[5]

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
↑ Stoykova S, Goranova Y, Pantcheva I, Atanasov V, Danchev D, Petrova S. Hemolytic activity and platelet aggregation inhibitory effect of vipoxin's basic sPLA2 subunit. Interdiscip Toxicol. 2013 Sep;6(3):136-40. doi: 10.2478/intox-2013-0021. PMID:24678250 doi:http://dx.doi.org/10.2478/intox-2013-0021
↑ 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
↑ Stoykova S, Goranova Y, Pantcheva I, Atanasov V, Danchev D, Petrova S. Hemolytic activity and platelet aggregation inhibitory effect of vipoxin's basic sPLA2 subunit. Interdiscip Toxicol. 2013 Sep;6(3):136-40. doi: 10.2478/intox-2013-0021. PMID:24678250 doi:http://dx.doi.org/10.2478/intox-2013-0021
↑ Georgieva DN, Rypniewski W, Gabdoulkhakov A, Genov N, Betzel C. Asp49 phospholipase A(2)-elaidoylamide complex: a new mode of inhibition. Biochem Biophys Res Commun. 2004 Jul 9;319(4):1314-21. PMID:15194511 doi:10.1016/j.bbrc.2004.05.106

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/1rgb"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1rgb]] is a 4 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=1RGB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RGB FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ELD:(9E)-OCTADEC-9-ENAMIDE'>ELD</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ELD:(9E)-OCTADEC-9-ENAMIDE'>ELD</scene></td></tr>
-<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rgb RCSB], [http://www.ebi.ac.uk/pdbsum/1rgb 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=1rgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rgb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rgb RCSB], [http://www.ebi.ac.uk/pdbsum/1rgb PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[Category: Vipera ammodytes meridionalis]]
-[[Category: Georgieva, D N.]]
+[[Category: Georgieva, D N]]
 [[Category: Elaidoylamide]]
 [[Category: Hydrolase]]
 [[Category: Neurotoxin]]
 [[Category: Phospholipase a2]]

1rgb

From Proteopedia

Revision as of 15:50, 25 December 2014

Phospholipase A2 from Vipera ammodytes meridionalis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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