5x79
From Proteopedia
(Difference between revisions)
m (Protected "5x79" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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
| |||||||||||
