Structure of USP7 catalytic domain and three Ubl-domains reveals a connector α-helix with regulatory role

Journal of Structural Biology

Volumn 195, Issue 1, 2016, Pages 11-18

  Kim, Robbert Q ^a   van Dijk, Willem J ^a   Sixma, Titia K ^a  

^a NETHERLANDS CANCER INSTITUTE   (Netherlands)

Author keywords

Deubiquitination; Helix stability; Ubiquitin conjugation; USP7

Indexed keywords

DEUBIQUITINASE; UBIQUITIN LIKE PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; USP7 PROTEIN; UBIQUITIN CARBOXYL TERMINAL HYDROLASE 7; USP7 PROTEIN, HUMAN;

ALLOSTERISM; ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONJUGATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; STRUCTURE ANALYSIS; UBIQUITINATION; ALLOSTERIC SITE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC SITE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DEUBIQUITINATING ENZYMES; HUMANS; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN DOMAINS; PROTEIN STRUCTURE, SECONDARY; UBIQUITIN-SPECIFIC PEPTIDASE 7;

EID: 84969204392     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2016.05.005     Document Type: Article

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