18gs: Difference between revisions
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==GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE== | ==GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE== | ||
<StructureSection load='18gs' size='340' side='right' caption='[[18gs]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='18gs' size='340' side='right' caption='[[18gs]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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=18gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=18gs OCA], [http://pdbe.org/18gs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=18gs RCSB], [http://www.ebi.ac.uk/pdbsum/18gs PDBsum]</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=18gs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=18gs OCA], [http://pdbe.org/18gs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=18gs RCSB], [http://www.ebi.ac.uk/pdbsum/18gs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=18gs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 18gs" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 18gs" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:40, 15 November 2017
GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENEGLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH 1-(S-GLUTATHIONYL)-2,4-DINITROBENZENE
Structural highlights
Function[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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutathione S -transferases (GSTs) play a pivotal role in the detoxification of foreign chemicals and toxic metabolites. They were originally termed ligandins because of their ability to bind large molecules (molecular masses >400 Da), possibly for storage and transport roles. The location of the ligandin site in mammalian GSTs is still uncertain despite numerous studies in recent years. Here we show by X-ray crystallography that the ligandin binding site in human pi class GST P1-1 occupies part of one of the substrate binding sites. This work has been extended to the determination of a number of enzyme complex crystal structures which show that very large ligands are readily accommodated into this substrate binding site and in all, but one case, causes no significant movement of protein side-chains. Some of these molecules make use of a hitherto undescribed binding site located in a surface pocket of the enzyme. This site is conserved in most, but not all, classes of GSTs suggesting it may play an important functional role. The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site).,Oakley AJ, Lo Bello M, Nuccetelli M, Mazzetti AP, Parker MW J Mol Biol. 1999 Aug 27;291(4):913-26. PMID:10452896[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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