Dynamically-Driven Inactivation of the Catalytic Machinery of the SARS 3C-Like Protease by the N214A Mutation on the Extra Domain

Despite utilizing the same chymotrypsin fold to host the catalytic machinery, coronavirus 3C-like proteases (3CLpro) noticeably differ from picornavirus 3C proteases in acquiring an extra helical domain in evolution. Previously, the extra domain was demonstrated to regulate the catalysis of the SARS...

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Detalles Bibliográficos
Autores principales: Shi, Jiahai, Han, Nanyu, Lim, Liangzhong, Lua, Shixiong, Sivaraman, J., Wang, Lushan, Mu, Yuguang, Song, Jianxing
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044768/
https://www.ncbi.nlm.nih.gov/pubmed/21390281
http://dx.doi.org/10.1371/journal.pcbi.1001084

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3044768/
https://www.ncbi.nlm.nih.gov/pubmed/21390281
http://dx.doi.org/10.1371/journal.pcbi.1001084

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