Activation and maturation of SARS-CoV main protease

被引：96
|
作者：
Xia, Bin [1 ]
Kang, Xue
机构：
[1] Peking Univ, Beijing Nucl Magnet Resonance Ctr, Coll Chem & Mol Engn, Beijing 100871, Peoples R China
来源：
PROTEIN & CELL | 2011年 / 2卷 / 04期
关键词：
severe acute respiratory syndrome; M-pro; structure; dimerization; RESPIRATORY-SYNDROME CORONAVIRUS; 3C-LIKE PROTEASE; DIMER INTERFACE; M-PRO; DIMERIZATION; PROTEINASE; MECHANISM; DISSOCIATION; CATALYSIS; CLEAVAGE;
D O I：
10.1007/s13238-011-1034-1
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
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.
引用
收藏
页码：282 / 290
页数：9
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