From SARS to MERS : crystallographic studies on coronaviral proteases enable antiviral drug design
German Center for Infection Research · University of Lübeck
Abstract
This review focuses on the important contributions that macromolecular crystallography has made over the past 12 years to elucidating structures and mechanisms of the essential proteases of coronaviruses, the main protease (M(pro) ) and the papain-like protease (PL(pro) ). The role of X-ray crystallography in structure-assisted drug discovery against these targets is discussed. Aspects dealt with in this review include the emergence of the SARS coronavirus in 2002-2003 and of the MERS coronavirus 10 years later and the origins of these viruses. The crystal structure of the free SARS coronavirus M(pro) and its dependence on pH is discussed, as are efforts to design inhibitors on the basis of these structures.…
Citation impact
- FWCI
- 4.90
- Percentile
- 100%
- References
- 91
Authors
1Topics & keywords
- Coronavirus
- Proteases
- Protease
- Virology
- Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
- Biology
- Computational biology
- Mechanism (biology)
- Good health and well-being