2que: Difference between revisions

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[[Image:2que.jpg|left|200px]]


{{Structure
==Saturation of substrate-binding site using two natural ligands: Crystal structure of a ternary complex of phospholipase A2 with anisic acid and ajmaline at 2.25 A resolution==
|PDB= 2que |SIZE=350|CAPTION= <scene name='initialview01'>2que</scene>, resolution 2.25&Aring;
<StructureSection load='2que' size='340' side='right'caption='[[2que]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=AJM:AJMALINE'>AJM</scene> and <scene name='pdbligand=ANN:4-METHOXYBENZOIC ACID'>ANN</scene>
<table><tr><td colspan='2'>[[2que]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daboia_russelii_pulchella Daboia russelii pulchella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QUE FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AJM:AJMALINE'>AJM</scene>, <scene name='pdbligand=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene></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=2que FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2que OCA], [https://pdbe.org/2que PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2que RCSB], [https://www.ebi.ac.uk/pdbsum/2que PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2que ProSAT]</span></td></tr>
</table>
== 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/2que_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2que ConSurf].
<div style="clear:both"></div>


'''Saturation of substrate-binding site using two natural ligands: Crystal structure of a ternary complex of phospholipase A2 with anisic acid and ajmaline at 2.25 A resolution'''
==See Also==
 
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 
== References ==
==About this Structure==
<references/>
2QUE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_pulchella Daboia russellii pulchella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QUE OCA].
__TOC__
[[Category: Daboia russellii pulchella]]
</StructureSection>
[[Category: Phospholipase A(2)]]
[[Category: Daboia russelii pulchella]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kaur, P.]]
[[Category: Kaur P]]
[[Category: Kumar, S.]]
[[Category: Kumar S]]
[[Category: Sharma, S.]]
[[Category: Sharma S]]
[[Category: Singh, N.]]
[[Category: Singh N]]
[[Category: Singh, T P.]]
[[Category: Singh TP]]
[[Category: AJM]]
[[Category: ANN]]
[[Category: active site]]
[[Category: binding affinity]]
[[Category: calcium]]
[[Category: hydrolase]]
[[Category: lipid degradation]]
[[Category: lipid hydrolysis]]
[[Category: metal-binding]]
[[Category: neurotoxin]]
[[Category: presynaptic neurotoxin]]
[[Category: secreted]]
[[Category: toxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:29:45 2008''

Latest revision as of 11:35, 30 October 2024

Saturation of substrate-binding site using two natural ligands: Crystal structure of a ternary complex of phospholipase A2 with anisic acid and ajmaline at 2.25 A resolutionSaturation of substrate-binding site using two natural ligands: Crystal structure of a ternary complex of phospholipase A2 with anisic acid and ajmaline at 2.25 A resolution

Structural highlights

2que is a 1 chain structure with sequence from Daboia russelii pulchella. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
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

2que, resolution 2.25Å

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