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. 2011 Apr 28;2(4):282–290. doi: 10.1007/s13238-011-1034-1

Activation and maturation of SARS-CoV main protease

Bin Xia 1,, Xue Kang 1
PMCID: PMC4875205  PMID: 21533772

Abstract

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.

Keywords: severe acute respiratory syndrome, Mpro, structure, dimerization

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