1gum: Difference between revisions
New page: left|200px<br /> <applet load="1gum" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gum, resolution 3.0Å" /> '''HUMAN GLUTATHIONE TR... |
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==About this Structure== | ==About this Structure== | ||
1GUM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUM OCA]]. | 1GUM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 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 [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUM OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10329152 10329152] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10329152 10329152] | ||
[[Category: Glutathione transferase]] | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidative stress]] | [[Category: oxidative stress]] | ||
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Revision as of 09:10, 30 October 2007
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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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