Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 52, 2005, Pages 18890-18895

  Özkan, Engin ^a   Yu, Hongtao ^a   Deisenhofer, Johann ^a,b  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

E2 enzymes; E3 enzymes; Mechanism

Indexed keywords

BACTERIAL ENZYME; PROTEIN UBCH5B; RING TYPE UBIQUITIN LIGASE; THIOESTER; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN TARGETING; STRUCTURE ANALYSIS; UBIQUITINATION;

ALLOSTERIC SITE; BINDING SITES; CLUSTER ANALYSIS; CYCLIN B; CYSTEINE; ESCHERICHIA COLI; ESTERS; HUMANS; KINETICS; LIGASES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTAGENESIS; MUTATION; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; TIME FACTORS; UBIQUITIN; UBIQUITIN-ACTIVATING ENZYMES; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITIN-PROTEIN LIGASE COMPLEXES; UBIQUITIN-PROTEIN LIGASES;

BACTERIA (MICROORGANISMS);

EID: 30044437590     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0509418102     Document Type: Article

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