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1gum

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[[Category: oxidative stress]]
[[Category: oxidative stress]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:14:54 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:19:43 2007''

Revision as of 13:14, 30 October 2007


1gum, resolution 3.0Å

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HUMAN GLUTATHIONE TRANSFERASE A4-4 WITHOUT LIGANDS

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

1GUM is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Sites: GTA, GTB, GTC, GTD, GTE, GTF, GTG, GTH, HTA, HTB, HTC, HTD, HTE, HTF, HTG and HTH. 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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