3vbz: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3vbz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oxyuranus_scutellatus_scutellatus Oxyuranus scutellatus scutellatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VBZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3vbz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oxyuranus_scutellatus_scutellatus Oxyuranus scutellatus scutellatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VBZ FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vc0|3vc0]]</div></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]] 1.76&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3vbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbz OCA], [https://pdbe.org/3vbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vbz RCSB], [https://www.ebi.ac.uk/pdbsum/3vbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vbz 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=3vbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbz OCA], [https://pdbe.org/3vbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vbz RCSB], [https://www.ebi.ac.uk/pdbsum/3vbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vbz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PA22_OXYSC PA22_OXYSC]] Snake venom phospholipase A2 (PLA2) that shows high presynaptic neurotoxicity in vertebrata that is independent of catalytic activity (PubMed:2544597, PubMed:10548416 and PubMed:16669624), as well as local myotoxicity when intramuscularly injected into mice (PubMed:16669624). Blocks acetylcholine release in Aplysia neurons (PubMed:8583413), and potentiates proinflammatory cellular signaling (PubMed:12782627). Potentiates glutamate excitoxicity when coinjected into brain of rats (PubMed:10548416). May act by binding in a calcium-dependent fashion and with high affinity to a neuronal-type (N-type) PLA2 receptor, and with very high affinity to a muscle-type (M-type) PLA2 receptor. In vitro, shows a high-specific activity on E.coli membranes and is more efficient on the anionic phospholipid POPG than on the anionic phospholipid POPS or the zwitterionic phospholipid POPC. Exerts catalytically-independent anti-HIV (IC(50) is 35 nM) activity and catalytically-dependent antimalarial activity (IC(50) is 3.1 nM when tested on P.falciparum grown in serum that contains lipoproteins). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:10548416</ref> <ref>PMID:12782627</ref> <ref>PMID:16669624</ref> <ref>PMID:2160984</ref> <ref>PMID:2544597</ref> <ref>PMID:8583413</ref> 
[https://www.uniprot.org/uniprot/PA2HC_OXYSC PA2HC_OXYSC] Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium binding protein 49 (RCN2), a protein localized in the lumen of endoplasmic reticulum. Monomer (beta chain): Snake venom phospholipase A2 homolog that is neither toxic nor enzymatically active. Does not bind calcium.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oxyuranus scutellatus scutellatus]]
[[Category: Oxyuranus scutellatus scutellatus]]
[[Category: Beltramini, M]]
[[Category: Beltramini M]]
[[Category: Cendron, L]]
[[Category: Cendron L]]
[[Category: Micetic, I]]
[[Category: Micetic I]]
[[Category: Paoli, M]]
[[Category: Paoli M]]
[[Category: Polverino, P]]
[[Category: Polverino P]]
[[Category: Calcium binding]]
[[Category: Neurotoxin]]
[[Category: Phospholipase]]
[[Category: Phospholipase a2 fold]]
[[Category: Pla2 fold]]
[[Category: Secreted]]
[[Category: Taipoxin alpha subunit binding]]
[[Category: Taipoxin gamma subunit binding]]
[[Category: Toxin]]
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