The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase

Biochemical and Biophysical Research Communications

Volumn 339, Issue 3, 2006, Pages 865-872

  Wei, Ping ^a   Fan, Keqiang ^a,c   Chen, Hao ^a,b   Ma, Liang ^a   Huang, Changkang ^a   Tan, Lei ^a   Xi, Dong ^a   Li, Chunmei ^a   Liu, Ying ^a   Cao, Aoneng ^a   Lai, Luhua ^a,b  

^a PEKING UNIVERSITY   (China)

^b PEKING UNIVERSITY   (China)

^c INSTITUTE OF MICROBIOLOGY   (China)

Author keywords

3C like proteinase; Dimerization inhibitor; Mutational study; N terminal peptide; Peptide inhibitor; SARS coronavirus; Zhang Poorman plot

Indexed keywords

ARGININE; ENZYME INHIBITOR; METHIONINE; OCTAPEPTIDE; OCTAPEPTIDE N 8; PROTEINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ACCURACY; AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; DIMERIZATION; DISSOCIATION CONSTANT; DRUG DESIGN; DRUG DETERMINATION; DRUG POTENCY; DRUG SYNTHESIS; ENZYME ACTIVE SITE; ENZYME ASSAY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SARS CORONAVIRUS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; ULTRACENTRIFUGATION;

BINDING SITES; COMPUTER SIMULATION; CYSTEINE ENDOPEPTIDASES; DIMERIZATION; DRUG DESIGN; ENDOPEPTIDASES; ENZYME ACTIVATION; ENZYME INHIBITORS; MODELS, CHEMICAL; MODELS, MOLECULAR; PEPTIDES; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP; VIRAL PROTEINS;

CORONAVIRUS; SARS CORONAVIRUS;

EID: 28844479986     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.11.102     Document Type: Article

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