Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors-Reference-Cited by-同舟云学术

Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors

Published:2020-04-24 Issue:6489 Volume:368 Page:409-412
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Zhang Linlin¹²^ORCID,Lin Daizong¹³^ORCID,Sun Xinyuanyuan¹²^ORCID,Curth Ute⁴,Drosten Christian⁵^ORCID,Sauerhering Lucie⁶⁷^ORCID,Becker Stephan⁶⁷,Rox Katharina⁸⁹^ORCID,Hilgenfeld Rolf¹²^ORCID

Affiliation:

1. Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23562 Lübeck, Germany.

2. German Center for Infection Research (DZIF), Hamburg-Lübeck-Borstel-Riems Site, University of Lübeck, 23562 Lübeck, Germany.

3. Changchun Discovery Sciences Ltd., 789 Shunda Road, Changchun, Jilin 130012, China.

4. Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.

5. Institute of Virology, Charité Universitätsmedizin Berlin, 10117 Berlin, Germany.

6. Institute of Virology, University of Marburg, 35043 Marburg, Germany.

7. German Center for Infection Research (DZIF), Marburg-Gießen-Langen Site, University of Marburg, 35043 Marburg, Germany.

8. Department of Chemical Biology, Helmholtz Center for Infection Research (HZI), 38124 Braunschweig, Germany.

9. German Center for Infection Research (DZIF), Hannover-Braunschweig Site, Helmholtz Center for Infection Research, 38124 Braunschweig, Germany.

Abstract

Targeting a key enzyme in SARS-CoV-2 Scientists across the world are working to understand severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2), the virus that causes coronavirus disease 2019 (COVID-19). Zhang et al. determined the x-ray crystal structure of a key protein in the virus' life cycle: the main protease. This enzyme cuts the polyproteins translated from viral RNA to yield functional viral proteins. The authors also developed a lead compound into a potent inhibitor and obtained a structure with the inhibitor bound, work that may provide a basis for development of anticoronaviral drugs. Science , this issue p. 409

Funder

German Center for Infection Research

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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