Journal
PROTEIN & CELL
Volume 2, Issue 4, Pages 282-290Publisher
SPRINGEROPEN
DOI: 10.1007/s13238-011-1034-1
Keywords
severe acute respiratory syndrome; M-pro; structure; dimerization
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Funding
- National Basic Research Program of China (973 Project) [2003CB514104]
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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 (M-pro) 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, M-pro is first auto-cleaved out of polyproteins. The monomeric form of M-pro 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 M-pro over the past years.
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