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2vhf

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{{STRUCTURE_2vhf| PDB=2vhf | SCENE= }}
{{STRUCTURE_2vhf| PDB=2vhf | SCENE= }}
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'''STRUCTURE OF THE CYLD USP DOMAIN'''
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===STRUCTURE OF THE CYLD USP DOMAIN===
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==Overview==
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The tumor suppressor CYLD antagonizes NF-kappaB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesized in response to cytokine stimulation. Here we describe the crystal structure of the CYLD USP domain, revealing a distinctive architecture that provides molecular insights into its specificity toward Lys63-linked polyubiquitin. We identify regions of the USP domain responsible for this specificity and demonstrate endodeubiquitinase activity toward such chains. Pathogenic truncations of the CYLD C terminus, associated with the hypertrophic skin tumor cylindromatosis, disrupt the USP domain, accounting for loss of CYLD catalytic activity. A small zinc-binding B box domain, similar in structure to other crossbrace Zn-binding folds-including the RING domain found in E3 ubiquitin ligases-is inserted within the globular core of the USP domain. Biochemical and functional characterization of the B box suggests a role as a protein-interaction module that contributes to determining the subcellular localization of CYLD.
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(as it appears on PubMed at http://www.pubmed.gov), where 18313383 is the PubMed ID number.
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==About this Structure==
==About this Structure==
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[[Category: Usp domain]]
[[Category: Usp domain]]
[[Category: Zn-binding domain]]
[[Category: Zn-binding domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:48:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:59:39 2008''

Revision as of 05:59, 28 July 2008

Template:STRUCTURE 2vhf

STRUCTURE OF THE CYLD USP DOMAIN

Template:ABSTRACT PUBMED 18313383

About this Structure

2VHF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Polyubiquitin and Reveals a B Box Module., Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, Barford D, Mol Cell. 2008 Feb 29;29(4):451-64. PMID:18313383

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