title: Activation and maturation of SARS-CoV main protease.
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.
authors.affiliation: 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
authors.forename: Bin
authors.initials: B
authors.lastname: Xia
authors.forename: Xue
authors.initials: X
authors.lastname: Kang
mesh_terms: D000086782:Coronavirus 3C Proteases; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D004789:Enzyme Activation; D006801:Humans; D008958:Models, Molecular; D020815:Polyproteins / Q000737:chemistry / Q000378:metabolism; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry / Q000201:enzymology*; D045169:Severe Acute Respiratory Syndrome / Q000821:virology*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D020815:Polyproteins; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086782:Coronavirus 3C Proteases