1w6v

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[[Image:1w6v.gif|left|200px]]<br /><applet load="1w6v" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w6v.gif|left|200px]]
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caption="1w6v" />
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'''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15'''<br />
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{{Structure
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|PDB= 1w6v |SIZE=350|CAPTION= <scene name='initialview01'>1w6v</scene>
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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'''SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16298993 16298993]
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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]]
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[[Category: structural genomics]]
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[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:05 2008''
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''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


PDB ID 1w6v

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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

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