1gul
HUMAN GLUTATHIONE TRANSFERASE A4-4 COMPLEX WITH IODOBENZYL GLUTATHIONE
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OverviewOverview
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 StructureAbout 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].
ReferenceReference
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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