Architecture of the catalytic HPN motif is conserved in all E2 conjugating enzymes

Biochemical Journal

Volumn 445, Issue 2, 2012, Pages 167-174

  Cook, Benjamin W ^a   Shaw, Gary S ^a  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

Catalytic pocket; Hydrogen bonding; NMR spectroscopy; Structure; Ubiquitin

Indexed keywords

ASPARAGINE; CARBON 13; COMPLEMENTARY DNA; HISTIDINE; IMIDAZOLE; NITROGEN 15; PROLINE; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME E2;

AMINO ACID SEQUENCE; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; ENZYME ACTIVITY; ENZYME MECHANISM; HYDROGEN BOND; ISOTOPE LABELING; MOLECULAR INTERACTION; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CONSERVED SEQUENCE; HISTIDINE; HUMANS; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; UBIQUITIN; UBIQUITIN-CONJUGATING ENZYMES; UBIQUITINATION;

EID: 84863197977     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120504     Document Type: Article

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