20gs: Difference between revisions

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[[Image:20gs.jpg|left|200px]]
{{Seed}}
[[Image:20gs.png|left|200px]]


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{{STRUCTURE_20gs|  PDB=20gs  |  SCENE=  }}  
{{STRUCTURE_20gs|  PDB=20gs  |  SCENE=  }}  


'''GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE'''
===GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Ligand]]
[[Category: Ligand]]
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Revision as of 00:49, 28 July 2008

File:20gs.png

Template:STRUCTURE 20gs

GLUTATHIONE S-TRANSFERASE P1-1 COMPLEXED WITH CIBACRON BLUE

Template:ABSTRACT PUBMED 10452896

About this Structure

20GS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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