1ozu
From Proteopedia
(New page: 200px<br /> <applet load="1ozu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ozu, resolution 1.30Å" /> '''Crystal Structure o...) |
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| - | <applet load="1ozu" size=" | + | |
caption="1ozu, resolution 1.30Å" /> | caption="1ozu, resolution 1.30Å" /> | ||
'''Crystal Structure of Familial ALS Mutant S134N of human Cu,Zn Superoxide Dismutase (CuZnSOD) to 1.3A resolution'''<br /> | '''Crystal Structure of Familial ALS Mutant S134N of human Cu,Zn Superoxide Dismutase (CuZnSOD) to 1.3A resolution'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OZU 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] Full crystallographic information is available from [http:// | + | 1OZU 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 <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta barrel]] | [[Category: beta barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:38:01 2008'' |
Revision as of 14:38, 15 February 2008
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Crystal Structure of Familial ALS Mutant S134N of human Cu,Zn Superoxide Dismutase (CuZnSOD) to 1.3A resolution
Contents |
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. In all cases, non-native conformational changes permit a gain, of interaction between dimers that leads to higher-order arrays. Normal, beta-sheet-containing proteins avoid such self-association by preventing, their edge strands from making intermolecular interactions. Loss of this, protection through conformational rearrangement in the metal-deficient, enzyme could be a toxic property common to mutants of SOD1 linked to FALS.
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
1OZU is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 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
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