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Volumn 21, Issue 13, 2002, Pages 3213-3224
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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain
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Author keywords
3C like; Catalytic dyad; Coronavirus; Proteinase; X ray crystallography
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Indexed keywords
CHYMOTRYPSIN;
CYSTEINE;
GLUTAMINE;
HISTIDINE;
LEUCINE;
PROTEINASE;
UNCLASSIFIED DRUG;
VIRAL MAIN PROTEINASE;
VIRUS ENZYME;
ARTICLE;
CORONAVIRUS;
CRYSTAL STRUCTURE;
DIMERIZATION;
ENZYME ACTIVE SITE;
ENZYME STRUCTURE;
ENZYME SUBSTRATE;
GASTROENTERITIS;
MOLECULAR MODEL;
MOLECULAR STABILITY;
MUTAGENESIS;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
OPTICAL RESOLUTION;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN INTERACTION;
PROTEIN PROCESSING;
SEQUENCE HOMOLOGY;
VIRUS MORPHOLOGY;
AMINO ACID SEQUENCE;
BINDING SITES;
CHYMOTRYPSIN;
CRYSTALLOGRAPHY, X-RAY;
CYSTEINE ENDOPEPTIDASES;
DIMERIZATION;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT FUSION PROTEINS;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
TRANSMISSIBLE GASTROENTERITIS VIRUS;
CORONAVIRUS;
RNA VIRUSES;
TRANSMISSIBLE GASTROENTERITIS VIRUS;
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EID: 0036646055
PISSN: 02614189
EISSN: None
Source Type: Journal
DOI: 10.1093/emboj/cdf327 Document Type: Article |
Times cited : (551)
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References (61)
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