1oez
From Proteopedia
(New page: 200px<br /> <applet load="1oez" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oez, resolution 2.15Å" /> '''ZN HIS46ARG MUTANT ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OEZ 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 ZN and SO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OEZ OCA]]. | + | 1OEZ 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 ZN and SO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OEZ OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Superoxide dismutase]] | ||
[[Category: Antonyuk, S.]] | [[Category: Antonyuk, S.]] | ||
[[Category: Doucette, P.]] | [[Category: Doucette, P.]] | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
| - | ''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 11:44:10 2007'' |
Revision as of 09:39, 30 October 2007
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ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE
Overview
Mutations in the SOD1 gene cause the autosomal dominant, neurodegenerative, disorder familial amyotrophic lateral sclerosis (FALS). In spinal cord, neurons of human FALS patients and in transgenic mice expressing these, mutant proteins, aggregates containing FALS SOD1 are observed., Accumulation of SOD1 aggregates is believed to interfere with axonal, transport, protein degradation and anti-apoptotic functions of the, neuronal cellular machinery. Here we show that metal-deficient, pathogenic, SOD1 mutant proteins crystallize in three different crystal forms, all of, which reveal higher-order assemblies of aligned beta-sheets. Amyloid-like, filaments and water-filled nanotubes arise through extensive interactions, between loop and beta-barrel elements of neighboring mutant SOD1, molecules. ... [(full description)]
About this Structure
1OEZ is a [Single protein] structure of sequence from [Homo sapiens] with ZN and SO4 as [ligands]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS., Elam JS, Taylor AB, Strange R, Antonyuk S, Doucette PA, Rodriguez JA, Hasnain SS, Hayward LJ, Valentine JS, Yeates TO, Hart PJ, Nat Struct Biol. 2003 Jun;10(6):461-7. PMID:12754496
Page seeded by OCA on Tue Oct 30 11:44:10 2007
