The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism

Journal of Molecular Biology

Volumn 289, Issue 2, 1999, Pages 371-384

  Barbato, Gaetano ^a   Cicero, Daniel O ^a   Nardi, M Chiara ^a   Steinkühler, Christian ^a   Cortese, Riccardo ^a   De Francesco, Raffaele ^a   Bazzo, Renzo ^a  

^a IRBM   (Italy)

Author keywords

HCV; NMR; NS3; Serine proteinase; Structure

Indexed keywords

CHYMOTRYPSIN; SERINE PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; HEPATITIS C VIRUS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION;

HEPATITIS C VIRUS; RNA VIRUSES;

EID: 0033522886     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2745     Document Type: Article

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