Only one protomer is active in the dimer of SARS 3C-like proteinase

Journal of Biological Chemistry

Volumn 281, Issue 20, 2006, Pages 13894-13898

  Chen, Hao ^a,b   Wei, Ping ^a   Huang, Changkang ^a   Tan, Lei ^a   Liu, Ying ^a   Lai, Luhua ^a,b  

^a PEKING UNIVERSITY   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; COMPUTER SIMULATION; DIMERS; DISSOCIATION; DRUG THERAPY; EPIDEMIOLOGY; MOLECULAR DYNAMICS; MONOMERS; MUTAGENESIS; PULMONARY DISEASES;

MUTANTS; PROTOMERS; SEVERE ACUTE RESPIRATORY SYNDROM (SARS);

ENZYMES;

DIMER; HYBRID PROTEIN; MONOMER; MUTANT PROTEIN; PROTEINASE; SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS 3C LIKE PROTEINASE; UNCLASSIFIED DRUG; VIRUS ENZYME;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONFORMATIONAL TRANSITION; DIMERIZATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; HYDROPHOBICITY; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; SARS CORONAVIRUS; SEVERE ACUTE RESPIRATORY SYNDROME; SIMULATION; WILD TYPE;

BINDING SITES; CATALYSIS; COLORIMETRY; CRYSTALLIZATION; CYSTEINE ENDOPEPTIDASES; DIMERIZATION; ENDOPEPTIDASES; GLUTAMIC ACID; HYDROGEN BONDING; KINETICS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SARS VIRUS; SUBSTRATE SPECIFICITY; VIRAL PROTEINS;

SARS CORONAVIRUS;

EID: 33744945316     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M510745200     Document Type: Article

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