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

Kanchan Anand, John Ziebuhr, Parvesh Wadhwani, Jeroen R. Mesters, Rolf Hilgenfeld*

*Corresponding author for this work
514 Citations (Scopus)


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

Original languageEnglish
Issue number5626
Pages (from-to)1763-1767
Number of pages5
Publication statusPublished - 13.06.2003

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

Coronavirus related work

  • Research on SARS-CoV-2 / COVID-19


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