1w6v
From Proteopedia
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| - | [[Image:1w6v.gif|left|200px]] | + | [[Image:1w6v.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15''' | + | {{Structure |
| + | |PDB= 1w6v |SIZE=350|CAPTION= <scene name='initialview01'>1w6v</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W6V is a [ | + | 1W6V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6V OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16298993 16298993] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: endopeptidase]] | [[Category: endopeptidase]] | ||
[[Category: spine]] | [[Category: spine]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
[[Category: thiolesterase]] | [[Category: thiolesterase]] | ||
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[[Category: usp15]] | [[Category: usp15]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:52:59 2008'' |
Revision as of 12:53, 20 March 2008
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| Activity: | Ubiquitin thiolesterase, with EC number 3.1.2.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 14:52:59 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
