19gs: Difference between revisions

Revision as of 15:41, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:19gs.png

Template:STRUCTURE 19gs

GLUTATHIONE S-TRANSFERASE P1-1GLUTATHIONE S-TRANSFERASE P1-1

Template:ABSTRACT PUBMED 10452896

About this StructureAbout this Structure

19GS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jun 30 15:41:13 2008

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OCA

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-[[Image:19gs.gif|left|200px]]
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 {{STRUCTURE_19gs|  PDB=19gs  |  SCENE=  }}
-'''GLUTATHIONE S-TRANSFERASE P1-1'''
+===GLUTATHIONE S-TRANSFERASE P1-1===
-==Overview==
+<!--
-Glutathione 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 &gt;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 line below this paragraph, {{ABSTRACT_PUBMED_10452896}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10452896 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10452896}}
 ==About this Structure==
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 [[Category: Glutathione transferase]]
 [[Category: Ligand]]
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