1gul
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(New page: 200px<br /> <applet load="1gul" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gul, resolution 2.70Å" /> '''HUMAN GLUTATHIONE T...)
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Revision as of 15:30, 29 October 2007
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HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE
Overview
The oxidation of lipids and cell membranes generates cytotoxic compounds, implicated in the etiology of aging, cancer, atherosclerosis, neurodegenerative diseases, and other illnesses. Glutathione transferase, (GST) A4-4 is a key component in the defense against the products of this, oxidative stress because, unlike other Alpha class GSTs, GST A4-4 shows, high catalytic activity with lipid peroxidation products such as, 4-hydroxynon-2-enal (HNE). The crystal structure of human apo GST A4-4, unexpectedly possesses an ordered C-terminal alpha-helix, despite the, absence of any ligand. The structure of human GST A4-4 in complex with the, inhibitor S-(2-iodobenzyl) glutathione reveals key features of the, electrophilic substrate-binding pocket which confer specificity toward, HNE. Three ... [(full description)]
About this Structure
1GUL is a [Single protein] structure of sequence from [Homo sapiens] with 2IB as [ligand]. Active as [[1]], with EC number [2.5.1.18]. Full crystallographic information is available from [OCA].
Reference
Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products., Bruns CM, Hubatsch I, Ridderstrom M, Mannervik B, Tainer JA, J Mol Biol. 1999 May 7;288(3):427-39. PMID:10329152
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