Activation and maturation of SARS-CoV main protease.
10.1007/s13238-011-1034-1
- Author:
Bin XIA
1
;
Xue KANG
Author Information
1. Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, and School of Life Sciences, Peking University, Beijing 100871, China. binxia@pku.edu.cn
- Publication Type:Journal Article
- MeSH:
Crystallography, X-Ray;
Cysteine Endopeptidases;
chemistry;
metabolism;
Enzyme Activation;
Humans;
Models, Molecular;
Polyproteins;
chemistry;
metabolism;
Protein Multimerization;
Protein Structure, Tertiary;
SARS Virus;
chemistry;
enzymology;
Severe Acute Respiratory Syndrome;
virology;
Viral Proteins;
chemistry;
metabolism
- From:
Protein & Cell
2011;2(4):282-290
- CountryChina
- Language:English
-
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 (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.
