4fga: Difference between revisions
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New page: '''Unreleased structure''' The entry 4fga is ON HOLD Authors: Shukla, P.K., Sinha, M., Dey, S., Kaur, P., Sharma, S., Singh, T.P. Description: Design of peptide inhibitors of group II ... |
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==Design of peptide inhibitors of group II phospholipase A2: Crystal structure of the complex of phospholipsae A2 with a designed tripeptide, Ala- Tyr- Lys at 2.3 A resolution== | |||
<StructureSection load='4fga' size='340' side='right'caption='[[4fga]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fga]] is a 2 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=4FGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGA 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]] 2.3Å</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=4fga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fga OCA], [https://pdbe.org/4fga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fga RCSB], [https://www.ebi.ac.uk/pdbsum/4fga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fga 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> | |||
==See Also== | |||
*[[Phospholipase A2 3D structures|Phospholipase A2 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Daboia russelii pulchella]] | |||
[[Category: Large Structures]] | |||
[[Category: Dey S]] | |||
[[Category: Kaur P]] | |||
[[Category: Sharma S]] | |||
[[Category: Shukla PK]] | |||
[[Category: Singh TP]] | |||
[[Category: Sinha M]] | |||
Latest revision as of 13:51, 8 November 2023
Design of peptide inhibitors of group II phospholipase A2: Crystal structure of the complex of phospholipsae A2 with a designed tripeptide, Ala- Tyr- Lys at 2.3 A resolution
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