5x79: Difference between revisions
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==Human GST Pi conjugated with novel inhibitor, GS-ESF== | |||
<StructureSection load='5x79' size='340' side='right' caption='[[5x79]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5x79]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X79 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GF5:(2S)-2-azanyl-5-[[(2R)-3-(2-fluorosulfonylethylsulfanyl)-1-(2-hydroxy-2-oxoethylamino)-1-oxidanylidene-propan-2-yl]amino]-5-oxidanylidene-pentanoic+acid'>GF5</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x79 OCA], [http://pdbe.org/5x79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x79 RCSB], [http://www.ebi.ac.uk/pdbsum/5x79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x79 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We herein report the first covalent G-site-binding inhibitor for GST, GS-ESF (1), which irreversibly inhibited the GSTP1-1 function. LC-MS/MS and X-ray structure analyses of the covalently linked GST-inhibitor complex suggested that 1 reacted with Tyr108 of GSTP1-1. The mechanism of covalent bond formation was discussed based on MD simulation results. | |||
A covalent G-site inhibitor for glutathione S-transferase Pi (GSTP1-1).,Shishido Y, Tomoike F, Kimura Y, Kuwata K, Yano T, Fukui K, Fujikawa H, Sekido Y, Murakami-Tonami Y, Kameda T, Shuto S, Abe H Chem Commun (Camb). 2017 Aug 29. doi: 10.1039/c7cc05829b. PMID:28848941<ref>PMID:28848941</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5x79" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glutathione transferase]] | |||
[[Category: Abe, H]] | |||
[[Category: Fukui, K]] | |||
[[Category: Kimura, Y]] | |||
[[Category: Shishido, Y]] | |||
[[Category: Tomoike, F]] | |||
[[Category: Covalent inhibitor]] | |||
[[Category: Gstp]] | |||
[[Category: Transferase]] | |||
[[Category: Transferase-transferase inhibitor complex]] | |||
Revision as of 10:57, 13 September 2017
Human GST Pi conjugated with novel inhibitor, GS-ESF
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