1gul
From Proteopedia
(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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==About this Structure== | ==About this Structure== | ||
| - | 1GUL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with 2IB as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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=1GUL OCA]]. | + | 1GUL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with 2IB as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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=1GUL 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]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:15:33 2007'' |
Revision as of 09:10, 30 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 [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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