2aga

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[[Image:2aga.gif|left|200px]]
[[Image:2aga.gif|left|200px]]
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{{Structure
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|PDB= 2aga |SIZE=350|CAPTION= <scene name='initialview01'>2aga</scene>
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The line below this paragraph, containing "STRUCTURE_2aga", creates the "Structure Box" on the page.
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|GENE= ATXN3, ATX3, MJD, MJD1, SCA3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2aga| PDB=2aga | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aga OCA], [http://www.ebi.ac.uk/pdbsum/2aga PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aga RCSB]</span>
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'''De-ubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain'''
'''De-ubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain'''
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[[Category: Polo, S.]]
[[Category: Polo, S.]]
[[Category: Senic-Matuglia, F.]]
[[Category: Senic-Matuglia, F.]]
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[[Category: ataxia]]
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[[Category: Ataxia]]
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[[Category: polyglutamine]]
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[[Category: Polyglutamine]]
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[[Category: ubiquitin]]
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[[Category: Ubiquitin]]
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[[Category: uim]]
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[[Category: Uim]]
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[[Category: vcp/p97]]
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[[Category: Vcp/p97]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:00:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:52:19 2008''
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Revision as of 16:00, 3 May 2008

Image:2aga.gif

Template:STRUCTURE 2aga

De-ubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain


Overview

Spinocerebellar ataxia type 3 is a human neurodegenerative disease resulting from polyglutamine tract expansion. The affected protein, ataxin-3, which contains an N-terminal Josephin domain followed by tandem ubiquitin (Ub)-interacting motifs (UIMs) and a polyglutamine stretch, has been implicated in the function of the Ub proteasome system. NMR-based structural analysis has now revealed that the Josephin domain binds Ub and has a papain-like fold that is reminiscent of that of other deubiquitinases, despite primary sequence divergence but consistent with its deubiqutinating activity. Mutation of the catalytic Cys enhances the stability of a complex between ataxin-3 and polyubiquitinated proteins. This effect depends on the integrity of the UIM region, suggesting that the UIMs are bound to the substrate polyubiquitin during catalysis. We propose that ataxin-3 functions as a polyubiquitin chain-editing enzyme.

About this Structure

2AGA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain., Mao Y, Senic-Matuglia F, Di Fiore PP, Polo S, Hodsdon ME, De Camilli P, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12700-5. Epub 2005 Aug 23. PMID:16118278 Page seeded by OCA on Sat May 3 19:00:50 2008

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