1sv9: Difference between revisions

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<StructureSection load='1sv9' size='340' side='right'caption='[[1sv9]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
<StructureSection load='1sv9' size='340' side='right'caption='[[1sv9]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russellii_russellii Daboia russellii russellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SV9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russelii_russelii Daboia russelii russelii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SV9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIF:2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC+ACID'>DIF</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]] 2.71&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fb2|1fb2]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIF:2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC+ACID'>DIF</scene></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=1sv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sv9 OCA], [https://pdbe.org/1sv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1sv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sv9 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=1sv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sv9 OCA], [https://pdbe.org/1sv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1sv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sv9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PA2B8_DABRR PA2B8_DABRR]] Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18062812</ref> <ref>PMID:2115497</ref> <ref>PMID:8835338</ref>
[https://www.uniprot.org/uniprot/PA2B8_DABRR PA2B8_DABRR] Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.<ref>PMID:18062812</ref> <ref>PMID:2115497</ref> <ref>PMID:8835338</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Daboia russellii russellii]]
[[Category: Daboia russelii russelii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ethayathulla, A S]]
[[Category: Ethayathulla AS]]
[[Category: Sharma, S]]
[[Category: Prem kumar R]]
[[Category: Singh, N]]
[[Category: Senthil kumar R]]
[[Category: Singh, T P]]
[[Category: Sharma S]]
[[Category: Kumar, R Prem]]
[[Category: Singh N]]
[[Category: Kumar, R Senthil]]
[[Category: Singh TP]]
[[Category: 7a resolution]]
[[Category: Complex]]
[[Category: Diclofenac]]
[[Category: Phospholipase a2]]
[[Category: Toxin]]

Latest revision as of 09:20, 23 August 2023

Crystal structure of the complex formed between groupII phospholipase A2 and anti-inflammatory agent 2-[(2,6-Dichlorophenyl)amino] benzeneacetic acid at 2.7A resolutionCrystal structure of the complex formed between groupII phospholipase A2 and anti-inflammatory agent 2-[(2,6-Dichlorophenyl)amino] benzeneacetic acid at 2.7A resolution

Structural highlights

1sv9 is a 1 chain structure with sequence from Daboia russelii russelii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.71Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PA2B8_DABRR Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM) (PubMed:18062812). It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Faure G, Gowda VT, Maroun RC. Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics. BMC Struct Biol. 2007 Dec 6;7:82. PMID:18062812 doi:http://dx.doi.org/10.1186/1472-6807-7-82
  2. ↑ Kasturi S, Rudrammaji LM, Gowda TV. Antibodies to a phospholipase A2 from Vipera russelli selectively neutralize venom neurotoxicity. Immunology. 1990 Jun;70(2):175-80. PMID:2115497
  3. ↑ Tsai IH, Lu PJ, Su JC. Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies. Toxicon. 1996 Jan;34(1):99-109. PMID:8835338

1sv9, resolution 2.71Å

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