1tg4: Difference between revisions

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[[Image:1tg4.gif|left|200px]]


{{Structure
==Design of specific inhibitors of groupII phospholipase A2(PLA2): Crystal structure of the complex formed between russells viper PLA2 and designed peptide Phe-Leu-Ala-Tyr-Lys at 1.7A resolution==
|PDB= 1tg4 |SIZE=350|CAPTION= <scene name='initialview01'>1tg4</scene>, resolution 1.70&Aring;
<StructureSection load='1tg4' size='340' side='right'caption='[[1tg4]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1tg4]] is a 2 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=1TG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TG4 FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg4 OCA], [https://pdbe.org/1tg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tg4 RCSB], [https://www.ebi.ac.uk/pdbsum/1tg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tg4 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1skg|1SKG]], [[1tgm|1TGM]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg4 OCA], [http://www.ebi.ac.uk/pdbsum/1tg4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tg4 RCSB]</span>
== 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/tg/1tg4_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=1tg4 ConSurf].
<div style="clear:both"></div>


'''Design of specific inhibitors of groupII phospholipase A2(PLA2): Crystal structure of the complex formed between russells viper PLA2 and designed peptide Phe-Leu-Ala-Tyr-Lys at 1.7A resolution'''
==See Also==
 
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]]
 
== References ==
==About this Structure==
<references/>
1TG4 is a [[Single protein]] structure of sequence from [http://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=1TG4 OCA].
__TOC__
[[Category: Daboia russellii russellii]]
</StructureSection>
[[Category: Phospholipase A(2)]]
[[Category: Daboia russelii russelii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Betzel, C.]]
[[Category: Betzel C]]
[[Category: Dey, S.]]
[[Category: Dey S]]
[[Category: Ethayathulla, A S.]]
[[Category: Ethayathulla AS]]
[[Category: Perbandt, M.]]
[[Category: Perbandt M]]
[[Category: Sharma, S.]]
[[Category: Sharma S]]
[[Category: Singh, N.]]
[[Category: Singh N]]
[[Category: Singh, T P.]]
[[Category: Singh TP]]
[[Category: Somvanshi, R K.]]
[[Category: Somvanshi RK]]
[[Category: phospholipase a2,flayk,complex,specific inhibitor,crystal structure]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:35 2008''

Latest revision as of 10:28, 30 October 2024

Design of specific inhibitors of groupII phospholipase A2(PLA2): Crystal structure of the complex formed between russells viper PLA2 and designed peptide Phe-Leu-Ala-Tyr-Lys at 1.7A resolutionDesign of specific inhibitors of groupII phospholipase A2(PLA2): Crystal structure of the complex formed between russells viper PLA2 and designed peptide Phe-Leu-Ala-Tyr-Lys at 1.7A resolution

Structural highlights

1tg4 is a 2 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 1.7Å
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

1tg4, resolution 1.70Å

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