1w6v

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[[Image:1w6v.gif|left|200px]]
[[Image:1w6v.gif|left|200px]]
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{{Structure
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|PDB= 1w6v |SIZE=350|CAPTION= <scene name='initialview01'>1w6v</scene>
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The line below this paragraph, containing "STRUCTURE_1w6v", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </span>
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{{STRUCTURE_1w6v| PDB=1w6v | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6v OCA], [http://www.ebi.ac.uk/pdbsum/1w6v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w6v RCSB]</span>
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'''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15'''
'''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15'''
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Truffault, V.]]
[[Category: Truffault, V.]]
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[[Category: cleavage]]
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[[Category: Cleavage]]
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[[Category: deubiquitinating enzyme]]
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[[Category: Deubiquitinating enzyme]]
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[[Category: deubiquitylation]]
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[[Category: Deubiquitylation]]
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[[Category: dub]]
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[[Category: Dub]]
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[[Category: dub15]]
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[[Category: Dub15]]
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[[Category: dusp]]
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[[Category: Dusp]]
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[[Category: endopeptidase]]
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[[Category: Endopeptidase]]
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[[Category: spine]]
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[[Category: Spine]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: structural proteomics in europe]]
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[[Category: Structural proteomics in europe]]
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[[Category: thiolesterase]]
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[[Category: Thiolesterase]]
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[[Category: ubiquitin]]
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[[Category: Ubiquitin]]
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[[Category: ubiquitin carboxyterminal hydrolase]]
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[[Category: Ubiquitin carboxyterminal hydrolase]]
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[[Category: ubiquitin specific protease]]
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[[Category: Ubiquitin specific protease]]
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[[Category: ubp15]]
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[[Category: Ubp15]]
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[[Category: uch]]
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[[Category: Uch]]
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[[Category: usp]]
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[[Category: Usp]]
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[[Category: usp15]]
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[[Category: Usp15]]
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Revision as of 05:13, 13 April 2008

Template:STRUCTURE 1w6v

SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15


Overview

Ubiquitin-specific proteases (USPs) can remove covalently attached ubiquitin moieties from target proteins and regulate both the stability and ubiquitin-signaling state of their substrates. All USPs contain a conserved catalytic domain surrounded by one or more subdomains, some of which contribute to target recognition. One such specific subdomain, the DUSP domain (domain present in ubiquitin-specific proteases), is present in at least seven different human USPs that regulate the stability of or interact with the hypoxia-inducible transcription factor HIF1-alpha, the Von Hippel-Lindau protein (pVHL), cullin E3 ligases, and BRCA2. We describe the NMR solution structure of the DUSP domain of human USP15, recently implicated in COP9 (constitutive photomorphogenic gene 9)-signalosome regulation. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet. The DUSP domain displays a novel fold, an alpha/beta tripod (AB3). DUSP domain surface properties and previously described work suggest a potential role in protein/protein interaction or substrate recognition.

About this Structure

1W6V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the human ubiquitin-specific protease 15 DUSP domain., de Jong RN, Ab E, Diercks T, Truffault V, Daniels M, Kaptein R, Folkers GE, J Biol Chem. 2006 Feb 24;281(8):5026-31. Epub 2005 Nov 18. PMID:16298993 Page seeded by OCA on Sun Apr 13 08:13:18 2008

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