Author: Chang, Gu-Gang
Title: Quaternary Structure of the SARS Coronavirus Main Protease Cord-id: chmktbvl Document date: 2009_7_22
ID: chmktbvl
Snippet: The maturation of the SARS coronavirus (CoV) involves the autocleavage of polyproteins 1a and 1ab by a main protease and papain-like protease. The functional unit of the main protease is a dimer in which each subunit has a Cys145–His41 catalytic dyad, with His41 acting as a general base. There is also a close correlation between dimer formation and the enzyme catalytic activity. A flip-flop mechanism is proposed for the main protease, in which the two subunits are used alternately in acylation
Document: The maturation of the SARS coronavirus (CoV) involves the autocleavage of polyproteins 1a and 1ab by a main protease and papain-like protease. The functional unit of the main protease is a dimer in which each subunit has a Cys145–His41 catalytic dyad, with His41 acting as a general base. There is also a close correlation between dimer formation and the enzyme catalytic activity. A flip-flop mechanism is proposed for the main protease, in which the two subunits are used alternately in acylation and deacylation. Both the main protease and the papain-like protease are ideal targets for rational drug design strategies against SARS-CoV.
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