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New page: left|200px<br /><applet load="2que" size="450" color="white" frame="true" align="right" spinBox="true" caption="2que, resolution 2.25Å" /> '''Saturation of substr... |
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== | ==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== | ||
<StructureSection load='2que' size='340' side='right'caption='[[2que]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
[ | <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> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | |||
<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> | ||
[[ | |||
[ | |||
==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 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
FunctionPA2B8_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 AlsoReferences
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