Structure of the SARS coronavirus main proteinase as an active C 2 crystallographic dimer

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 61, Issue 11, 2005, Pages 964-966

  Xu, Ting ^a   Ooi, Amy ^a   Lee, Hooi Chen ^a   Wilmouth, Rupert ^a   Liu, Ding Xiang ^b   Lescar, Julien ^a  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

^b INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

CORONAVIRUS; SARS CORONAVIRUS;

3C LIKE PROTEASE, SARS CORONAVIRUS; 3C-LIKE PROTEASE, SARS CORONAVIRUS; CYSTEINE PROTEINASE; DNA FRAGMENT; ENZYME INHIBITOR; VIRUS PROTEIN;

ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYME ACTIVE SITE; ENZYMOLOGY; METABOLISM; PH; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SARS CORONAVIRUS; STATISTICAL MODEL; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; DIMERIZATION; DNA FRAGMENTATION; ENZYME INHIBITORS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MODELS, STATISTICAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SARS VIRUS; VIRAL PROTEINS;

EID: 33744470114     PISSN: 17443091     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309105033257     Document Type: Article

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