Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination

Journal of Biological Chemistry

Volumn 286, Issue 47, 2011, Pages 40934-40942

  Liu, Jin ^a   Nussinov, Ruth ^a,b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; CULLINS; DIFFERENT SUBSTRATES; E3 UBIQUITIN LIGASES; LIGASES; MOLECULAR DYNAMICS SIMULATIONS; N-TERMINAL DOMAINS; POLYUBIQUITIN; POLYUBIQUITINATION; RIGID SCAFFOLDS; SCAFFOLD PROTEIN; SUBSTRATE DISTANCE; SUBSTRATE-BINDING; TRANSFER REACTION; UBIQUITIN; UBIQUITINATION;

ENZYMES; MOLECULAR DYNAMICS; PROTEINS; REACTION KINETICS; SCAFFOLDS (BIOLOGY);

SUBSTRATES;

CUL1 PROTEIN; CUL4A PROTEIN; CUL5 PROTEIN; CULLIN; SCAFFOLD PROTEIN; UBIQUITIN CONJUGATING ENZYME E2; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; HUMAN; MOLECULAR DYNAMICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; UBIQUITINATION;

ALLOSTERIC REGULATION; CULLIN PROTEINS; HUMANS; MOLECULAR DYNAMICS SIMULATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

EID: 81755171430     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.277236     Document Type: Article

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