Structure and dynamics of SARS coronavirus main proteinase (M pro)

Rolf Hilgenfeld*, Kanchan Anand, Jeroen R. Mesters, Zihe Rao, Xu Shen, Hualiang Jiang, Jinzhi Tan, Koen H.G. Verschueren

*Corresponding author for this work
5 Citations (Scopus)


All protein functions required for SARS coronavirus replication are encoded by the replicase gene.1,2 This gene encodes two overlapping polyproteins (pp1a and pp1ab), from which the functional proteins are released by extensive proteolytic processing. This is primarily achieved by the 34-kDa main proteinase (Mpro), which is frequently also called 3C-like proteinase (3CLpro) to indicate a similarity in substrate specificity with the 3C proteinase of picornaviruses.3 While useful at the time of initial description of the coronaviral enzyme, there are in fact large differences between the structures and mechanisms of these enzymes, making the designation of the coronavirus main proteinase as 3CLpro rather misleading. We will therefore use the term Mpro exclusively.
Original languageEnglish
Title of host publicationThe Nidoviruses : Toward Control of SARS and other Nidovirus Diseases
Number of pages7
PublisherSpringer New York LLC
Publication date01.01.2006
ISBN (Print)978-0-387-26202-4
ISBN (Electronic)978-0-387-33012-9
Publication statusPublished - 01.01.2006

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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