2oub: Difference between revisions

Revision as of 12:09, 18 October 2017

Crystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolutionCrystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolution

Structural highlights

2oub is a 1 chain structure with sequence from Daboia pulchella. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2o1n, 2arm
Activity:	Phospholipase A(2), with EC number 3.1.1.4
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.

References

↑ 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
↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[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

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolution==
 <StructureSection load='2oub' size='340' side='right' caption='[[2oub]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o1n|2o1n]], [[2arm|2arm]]</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=2oub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oub OCA], [http://pdbe.org/2oub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oub RCSB], [http://www.ebi.ac.uk/pdbsum/2oub 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=2oub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oub OCA], [http://pdbe.org/2oub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oub RCSB], [http://www.ebi.ac.uk/pdbsum/2oub PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oub ProSAT]</span></td></tr>
 </table>
 == Function ==

2oub: Difference between revisions

Revision as of 12:09, 18 October 2017

Crystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolutionCrystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolution

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

2oub: Difference between revisions

Revision as of 12:09, 18 October 2017

Crystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolutionCrystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolution

Structural highlights

Function

Evolutionary Conservation

See Also

References

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Search