Structure of a HOIP/E2∼ubiquitin complex reveals RBR E3 ligase mechanism and regulation

Nature

Volumn 529, Issue 7587, 2016, Pages 546-550

  Lechtenberg, Bernhard C ^a   Rajput, Akhil ^a   Sanishvili, Ruslan ^b   Dobaczewska, Małgorzata K ^a   Ware, Carl F ^a   Mace, Peter D ^c   Riedl, Stefan J ^a  

^a BURNHAM INSTITUTE   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

PARKIN; RING BETWEEN RING PROTEIN; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; MULTIPROTEIN COMPLEX; RNF31 PROTEIN, HUMAN; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

ARTIFICIAL SUBSTRATE; CATALYSIS; CELLS AND CELL COMPONENTS; ENZYME; ENZYME ACTIVITY; GENE;

ALLOSTERISM; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTALLIZATION; ENZYME CONFORMATION; GENE MUTATION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RING FINGER MOTIF; TRANSESTERIFICATION; CHEMISTRY; ENZYME ACTIVE SITE; HUMAN; METABOLISM; MOLECULAR MODEL; PROTEIN MOTIF; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC REGULATION; AMINO ACID MOTIFS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; RING FINGER DOMAINS; UBIQUITIN; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITIN-PROTEIN LIGASES;

EID: 84956664551     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature16511     Document Type: Article

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