2oub: Difference between revisions

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New page: left|200px<br /><applet load="2oub" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oub, resolution 2.75Å" /> '''Crystal structure of...
 
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[[Image:2oub.gif|left|200px]]<br /><applet load="2oub" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2oub, resolution 2.75&Aring;" />
'''Crystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolution'''<br />


==About this Structure==
==Crystal structure of the complex formed between phospholipase A2 and atenolol at 2.75 A resolution==
2OUB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Daboia_russellii_pulchella Daboia russellii pulchella] with 2TN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OUB OCA].
<StructureSection load='2oub' size='340' side='right'caption='[[2oub]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
[[Category: Daboia russellii pulchella]]
== Structural highlights ==
[[Category: Phospholipase A(2)]]
<table><tr><td colspan='2'>[[2oub]] 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=2OUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUB FirstGlance]. <br>
[[Category: Single protein]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
[[Category: Kaur, P.]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2TN:2-(4-(2-HYDROXY-3-(ISOPROPYLAMINO)PROPOXY)PHENYL)ETHANAMIDE'>2TN</scene></td></tr>
[[Category: Kumar, S.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oub OCA], [https://pdbe.org/2oub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oub RCSB], [https://www.ebi.ac.uk/pdbsum/2oub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oub ProSAT]</span></td></tr>
[[Category: Sharma, S.]]
</table>
[[Category: Singh, N.]]
== Function ==
[[Category: Singh, T.P.]]
[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>
[[Category: 2TN]]
== Evolutionary Conservation ==
[[Category: complex]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: inhibition]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2oub_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=2oub ConSurf].
<div style="clear:both"></div>


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:19:05 2007''
==See Also==
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Daboia russelii pulchella]]
[[Category: Large Structures]]
[[Category: Kaur P]]
[[Category: Kumar S]]
[[Category: Sharma S]]
[[Category: Singh N]]
[[Category: Singh TP]]

Latest revision as of 08:24, 17 October 2024

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 russelii pulchella. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
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

2oub, resolution 2.75Å

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