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

doi:10.1007/978-0-387-33012-9_106

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

Institute of Biochemistry

Tsinghua University

5 Citations (Scopus)

Abstract

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 language	English
Title of host publication	The Nidoviruses : Toward Control of SARS and other Nidovirus Diseases
Number of pages	7
Volume	581
Publisher	Springer New York LLC
Publication date	01.01.2006
Pages	585-591
ISBN (Print)	978-0-387-26202-4
ISBN (Electronic)	978-0-387-33012-9
DOIs	https://doi.org/10.1007/978-0-387-33012-9_106
Publication status	Published - 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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1007/978-0-387-33012-9_106

Cite this

Hilgenfeld, R., Anand, K., Mesters, J. R., Rao, Z., Shen, X., Jiang, H., Tan, J., & Verschueren, K. H. G. (2006). Structure and dynamics of SARS coronavirus main proteinase (M ^pro). In The Nidoviruses: Toward Control of SARS and other Nidovirus Diseases (Vol. 581, pp. 585-591). (Advances in Experimental Medicine and Biology; Vol. 581). Springer New York LLC. https://doi.org/10.1007/978-0-387-33012-9_106

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abstract = "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.",

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Hilgenfeld, R, Anand, K, Mesters, JR, Rao, Z, Shen, X, Jiang, H, Tan, J & Verschueren, KHG 2006, Structure and dynamics of SARS coronavirus main proteinase (M ^pro). in The Nidoviruses: Toward Control of SARS and other Nidovirus Diseases. vol. 581, Advances in Experimental Medicine and Biology, vol. 581, Springer New York LLC, pp. 585-591. https://doi.org/10.1007/978-0-387-33012-9_106

Structure and dynamics of SARS coronavirus main proteinase (M ^pro). / Hilgenfeld, Rolf; Anand, Kanchan; Mesters, Jeroen R. et al.
The Nidoviruses: Toward Control of SARS and other Nidovirus Diseases. Vol. 581 Springer New York LLC, 2006. p. 585-591 (Advances in Experimental Medicine and Biology; Vol. 581).

Research output: Chapters in Books/Reports/Conference Proceedings › Conference contribution › peer-review

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AU - Anand, Kanchan

AU - Mesters, Jeroen R.

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AU - Tan, Jinzhi

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