Residues on the dimer interface of SARS coronavirus 3C-like protease: Dimer stability characterization and enzyme catalytic activity analysis

Journal of Biochemistry

Volumn 143, Issue 4, 2008, Pages 525-536

  Chen, Shuai ^a   Zhang, Jian ^a   Hu, Tiancen ^a   Chen, Kaixian ^a   Jiang, Hualiang ^a   Shen, Xu ^a  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

Author keywords

Catalytic mechanism; Dimer interface; Dimerization activity relationship; Residue residue interactions; Site directed mutagenesis

Indexed keywords

PROTEIN 3C LIKE PROTEASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CATALYSIS; CONTROLLED STUDY; CROSS LINKING; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVITY; GENE MUTATION; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STABILITY; SARS CORONAVIRUS; SIMULATION;

BASE SEQUENCE; CATALYSIS; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; CYSTEINE ENDOPEPTIDASES; DIMERIZATION; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME STABILITY; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; VIRAL PROTEINS;

SARS CORONAVIRUS;

EID: 41349090332     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm246     Document Type: Article

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