Activation and maturation of SARS-CoV main protease
Identifieur interne : 001416 ( Main/Exploration ); précédent : 001415; suivant : 001417Activation and maturation of SARS-CoV main protease
Auteurs : Bin Xia ; Xue KangSource :
- Protein & Cell [ 1674-800X ] ; 2011.
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.
Url:
DOI: 10.1007/s13238-011-1034-1
PubMed: 21533772
PubMed Central: 4875205
Affiliations:
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Le document en format XML
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