1w6v: Difference between revisions
New page: left|200px<br /> <applet load="1w6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w6v" /> '''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HU... |
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'''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15'''<br /> | '''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15'''<br /> | ||
==Overview== | ==Overview== | ||
Ubiquitin-specific proteases (USPs) can remove covalently attached | 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== | ==About this Structure== | ||
1W6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http:// | 1W6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6V OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Daniels, M.]] | [[Category: Daniels, M.]] | ||
[[Category: Diercks, T.]] | [[Category: Diercks, T.]] | ||
[[Category: Folkers, G | [[Category: Folkers, G E.]] | ||
[[Category: Jong, R | [[Category: Jong, R D.De.]] | ||
[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: SPINE, Structural | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Truffault, V.]] | [[Category: Truffault, V.]] | ||
[[Category: cleavage]] | [[Category: cleavage]] | ||
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[[Category: usp15]] | [[Category: usp15]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:05 2008'' | ||
Revision as of 13:41, 21 February 2008
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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. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 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
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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 genomics
- Structural proteomics in europe
- Thiolesterase
- Ubiquitin
- Ubiquitin carboxyterminal hydrolase
- Ubiquitin specific protease
- Ubp15
- Uch
- Usp
- Usp15
