Article
Mechanism for controlling the monomer-dimer conversion of SARS coronavirus main protease.
Acta crystallographica. Section D, Biological crystallography - 1 May 2013
Wu Cheng Guo, Cheng Shu Chun, Chen Shiang Chuan, Li Juo Yan, Fang Yi Hsuan, Chen Yau Hung, Chou Chi Yuan
Abstract excerpt
The Severe acute respiratory syndrome coronavirus (SARS-CoV) main protease (M(pro)) cleaves two virion polyproteins (pp1a and pp1ab); this essential process represents an attractive target for the development of anti-SARS drugs. The functional unit of M(pro) is a homodimer and each subunit contains a His41/Cys145 catalytic dyad. Large amounts of biochemical and structural information are available on M(pro);...
Topics
- Binding Sites
- Coronavirus 3C Proteases
- Coronavirus M Proteins
- Crystallography, X-Ray
- Cysteine Endopeptidases
- Models, Molecular
- Mutation
- Protein Conformation
- Protein Multimerization
- Severe acute respiratory syndrome-related coronavirus