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

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie

Tsinghua University

5 Zitate (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.

Originalsprache	Englisch
Titel	The Nidoviruses : Toward Control of SARS and other Nidovirus Diseases
Seitenumfang	7
Band	581
Herausgeber (Verlag)	Springer New York LLC
Erscheinungsdatum	01.01.2006
Seiten	585-591
ISBN (Print)	978-0-387-26202-4
ISBN (elektronisch)	978-0-387-33012-9
DOIs	https://doi.org/10.1007/978-0-387-33012-9_106
Publikationsstatus	Veröffentlicht - 01.01.2006

Strategische Forschungsbereiche und Zentren

Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

Coronavirus-Bezug

Forschung zu SARS-CoV-2 / COVID-19

UN SDGs

Dieser Output leistet einen Beitrag zu folgendem(n) Ziel(en) für nachhaltige Entwicklung

Dokumente

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

Weitere Links

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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 (Band 581, S. 585-591). (Advances in Experimental Medicine and Biology; Band 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. Bd. 581, Advances in Experimental Medicine and Biology, Bd. 581, Springer New York LLC, S. 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. Band 581 Springer New York LLC, 2006. S. 585-591 (Advances in Experimental Medicine and Biology; Band 581).

Publikation: Kapitel in Büchern/Berichten/Konferenzbänden › Konferenzbeitrag › Begutachtung

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T1 - Structure and dynamics of SARS coronavirus main proteinase (M pro)

AU - Hilgenfeld, Rolf

AU - Anand, Kanchan

AU - Mesters, Jeroen R.

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AU - Shen, Xu

AU - Jiang, Hualiang

AU - Tan, Jinzhi

AU - Verschueren, Koen H.G.

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AB - 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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