Coronavirus Main Proteinase (3CL pro ) Structure: Basis for Design of Anti-SARS Drugs-Reference-Cited by-同舟云学术

Coronavirus Main Proteinase (3CL pro ) Structure: Basis for Design of Anti-SARS Drugs

Published:2003-06-13 Issue:5626 Volume:300 Page:1763-1767
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Anand Kanchan¹²³⁴,Ziebuhr John¹²³⁴,Wadhwani Parvesh¹²³⁴,Mesters Jeroen R.¹²³⁴,Hilgenfeld Rolf¹²³⁴

Affiliation:

1. Institute of Biochemistry, University of Lübeck, D-23538 Lübeck, Germany.

2. Institute of Molecular Biotechnology, D-07745 Jena, Germany.

3. Institute of Virology and Immunology, University of Würzburg, D-97078 Würzburg, Germany.

4. Institute of Molecular Biology, University of Jena, D-07745 Jena, Germany.

Abstract

A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (M pro , also called 3CL pro ), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) M pro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] M pro , and we constructed a homology model for SARS coronavirus (SARS-CoV) M pro . The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV M pro -mediated cleavage of a TGEV M pro substrate. Molecular modeling suggests that available rhinovirus 3C pro inhibitors may be modified to make them useful for treating SARS.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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