Coronavirus main proteinase (3CLpro) Structure: Basis for design of anti-SARS drugs

Science

Volumn 300, Issue 5626, 2003, Pages 1763-1767

  Anand, Kanchan ^a,b   Ziebuhr, John ^c   Wadhwani, Parvesh ^d   Mesters, Jeroen R ^a,b   Hilgenfeld, Rolf ^a,b  

^a UNIVERSITY OF LÜBECK   (Germany)

^b FRITZ LIPMANN INSTITUTE   (Germany)

^c UNIVERSITY OF WÜRZBURG   (Germany)

^d FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; PULMONARY DISEASES; VIRUSES;

SEVERE ACUTE RESPIRATORY SYNDROME (SARS);

ENZYMES;

PROTEINASE; VIRUS PROTEIN;

DRUG DEVELOPMENT; RESPIRATORY DISEASE; VIRUS;

ARTICLE; BINDING SITE; CORONAVIRUS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PORCINE CORONAVIRUS; PRIORITY JOURNAL; RHINOVIRUS; SARS CORONAVIRUS; SEVERE ACUTE RESPIRATORY SYNDROME; TRANSMISSIBLE GASTROENTERITIS VIRUS; VIRUS REPLICATION; VIRUS STRAIN;

AMINO ACID CHLOROMETHYL KETONES; AMINO ACID SEQUENCE; ANTIVIRAL AGENTS; BINDING SITES; CATALYTIC DOMAIN; CORONAVIRUS 229E, HUMAN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DIMERIZATION; DRUG DESIGN; HUMANS; ISOXAZOLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRROLIDINONES; RECOMBINANT PROTEINS; SARS VIRUS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SEVERE ACUTE RESPIRATORY SYNDROME; TRANSMISSIBLE GASTROENTERITIS VIRUS;

CORONAVIRUS; HUMAN CORONAVIRUS; HUMAN CORONAVIRUS 229E; RHINOVIRUS; SARS CORONAVIRUS; SARS COV; SUIDAE; TRANSMISSIBLE GASTROENTERITIS VIRUS;

EID: 0038120984     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1085658     Document Type: Article

References (24)

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14. free = 28.0%. For a description of structure elucidation, see the supporting online material.
15. J. Ziebuhr, G. Heusipp, S. G. Siddeli, J. Virol. 71, 3992 (1997).
16. pro, residues 301 and 302 are disordered and are not seen in the electron density.
17. S. G. Siddell, in The Coronavirdie, S. G. Siddell, Ed. (Plenum, New York, 1995), p. 1.
18. ro used corresponds to pp1a/pp1ab residues 3241 to 3544 of SARS-CoV strain TOR2 (National Center for Biotechnology Information accession number AY274119).
19. free = 23.5%. For a description of structure elucidation, see the supporting online material.
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21. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Glu; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
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23. M. D. Ryan, M. Flint, J. Gen. Virol. 78, 699 (1997).
24. pro have been deposited with the Research Collaboratory for Structural Bioinformatics Protein Data Bank under arcession numbers 1P9S, 1P9U, and 1P9T. 1P9T can be downloaded from ftp://ftp.rcsb.org/pub/pdb/ data/structures/models/current/pdb/p9.