Article
Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure.
Virology - 5 Jun 2009
Hu Tiancen, Zhang Yu, Li Lianwei, Wang Kuifeng, Chen Shuai, Chen Jing, Ding Jianping, Jiang Hualiang, Shen Xu
Abstract excerpt
The 3C-like protease of SARS coronavirus (SARS-CoV 3CL(pro)) is vital for SARS-CoV replication and is a promising drug target. It has been extensively proved that only the dimeric enzyme is active. Here we discovered that two adjacent mutations (Ser139_Ala and Phe140_Ala) on the dimer interface resulted in completely different crystal structures of the enzyme, demonstrating the distinct roles of these two...
Topics
- Coronavirus 3C Proteases
- Cysteine Endopeptidases
- Dimerization
- Models, Molecular
- Mutation
- Protein Structure, Tertiary
- Severe acute respiratory syndrome-related coronavirus
- Structure-Activity Relationship
- Viral Proteins