1w6v
From Proteopedia
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| - | | | + | {{STRUCTURE_1w6v| PDB=1w6v | SCENE= }} |
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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.]] | ||
| - | [[Category: | + | [[Category: Cleavage]] |
| - | [[Category: | + | [[Category: Deubiquitinating enzyme]] |
| - | [[Category: | + | [[Category: Deubiquitylation]] |
| - | [[Category: | + | [[Category: Dub]] |
| - | [[Category: | + | [[Category: Dub15]] |
| - | [[Category: | + | [[Category: Dusp]] |
| - | [[Category: | + | [[Category: Endopeptidase]] |
| - | [[Category: | + | [[Category: Spine]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Structural proteomics in europe]] |
| - | [[Category: | + | [[Category: Thiolesterase]] |
| - | [[Category: | + | [[Category: Ubiquitin]] |
| - | [[Category: | + | [[Category: Ubiquitin carboxyterminal hydrolase]] |
| - | [[Category: | + | [[Category: Ubiquitin specific protease]] |
| - | [[Category: | + | [[Category: Ubp15]] |
| - | [[Category: | + | [[Category: Uch]] |
| - | [[Category: | + | [[Category: Usp]] |
| - | [[Category: | + | [[Category: Usp15]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:13:18 2008'' | |
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Revision as of 05:13, 13 April 2008
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
Categories: Homo sapiens | Single protein | Ubiquitin thiolesterase | Ab, E. | Daniels, M. | Diercks, T. | Folkers, G E. | Jong, R D.De. | Kaptein, R. | SPINE, Structural Proteomics in Europe. | Truffault, V. | Cleavage | Deubiquitinating enzyme | Deubiquitylation | Dub | Dub15 | Dusp | Endopeptidase | Spine | Structural genomic | Structural proteomics in europe | Thiolesterase | Ubiquitin | Ubiquitin carboxyterminal hydrolase | Ubiquitin specific protease | Ubp15 | Uch | Usp | Usp15
