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| {{STRUCTURE_2vhf| PDB=2vhf | SCENE= }} | | {{STRUCTURE_2vhf| PDB=2vhf | SCENE= }} |
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| '''STRUCTURE OF THE CYLD USP DOMAIN'''
| | ===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. | | The line below this paragraph, {{ABSTRACT_PUBMED_18313383}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18313383 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18313383}} |
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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]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:48:53 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:59:39 2008'' |
