Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming

Nature Structural and Molecular Biology

Volumn 20, Issue 6, 2013, Pages 696-701

  Maspero, Elena ^a   Valentini, Eleonora ^a   Mari, Sara ^a   Cecatiello, Valentina ^b   Soffientini, Paolo ^a   Pasqualato, Sebastiano ^b   Polo, Simona ^a,c  

^a FIRC INSTITUTE OF MOLECULAR ONCOLOGY   (Italy)

^b EUROPEAN INSTITUTE OF ONCOLOGY   (Italy)

^c UNIVERSITY OF MILAN   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN PROTEIN LIGASE NEDD4;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFORMATIONAL TRANSITION; DOWN REGULATION; ENZYME CONFORMATION; ENZYME STRUCTURE; HOMOLOGOUS TO E6 AP C TERMINUS; HUMAN; HUMAN CELL; LIGATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROCESSING;

CRYSTALLOGRAPHY, X-RAY; ENDOSOMAL SORTING COMPLEXES REQUIRED FOR TRANSPORT; HUMANS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

EID: 84878900697     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2566     Document Type: Article

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