This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1w6v
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1w6v.gif|left|200px]] | + | [[Image:1w6v.gif|left|200px]] |
| - | + | ||
| - | '''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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 30: | Line 39: | ||
[[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]] | ||
| Line 41: | Line 50: | ||
[[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
| |||||||
| 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
