The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Polyubiquitin and Reveals a B Box Module

Molecular Cell

Volumn 29, Issue 4, 2008, Pages 451-464

  Komander, David ^a   Lord, Christopher J ^a   Scheel, Hartmut ^b   Swift, Sally ^a   Hofmann, Kay ^b   Ashworth, Alan ^a   Barford, David ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^b MILTENYI BIOTEC GMBH   (Germany)

Author keywords

PROTEINS

Indexed keywords

LYSINE; POLYUBIQUITIN; PROTEIN INTERACTING WITH PROTEIN KINASE C; TUMOR SUPPRESSOR PROTEIN; TUMOR SUPPRESSOR PROTEIN CYLD; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; ZINC BINDING PROTEIN;

ANIMAL CELL; ARTICLE; BIOCHEMISTRY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELLULAR DISTRIBUTION; CYLINDROMA; EMBRYO; ENZYME ACTIVITY; GENE INSERTION; HUMAN; HUMAN CELL; NONHUMAN; PATHOGENESIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SKIN HYPERTROPHY; SKIN TUMOR;

AMINO ACID SEQUENCE; BINDING SITES; CELL LINE; CRYSTALLOGRAPHY, X-RAY; GENES, TUMOR SUPPRESSOR; HUMANS; JNK MITOGEN-ACTIVATED PROTEIN KINASES; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NEOPLASMS; NF-KAPPA B; POLYUBIQUITIN; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN THIOLESTERASE; ZINC;

EID: 39549106692     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.12.018     Document Type: Article

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