Protein & Cell

, Volume 2, Issue 4, pp 282–290

Activation and maturation of SARS-CoV main protease


DOI: 10.1007/s13238-011-1034-1

Cite this article as:
Xia, B. & Kang, X. Protein Cell (2011) 2: 282. doi:10.1007/s13238-011-1034-1


The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (Mpro) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, Mpro is first auto-cleaved out of polyproteins. The monomeric form of Mpro is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of Mpro over the past years.


severe acute respiratory syndrome Mpro structure dimerization 

Copyright information

© Higher Education Press and Springer-Verlag Berlin Heidelberg 2011

Authors and Affiliations

  1. 1.Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, and School of Life SciencesPeking UniversityBeijingChina

Personalised recommendations