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...
Guardado en:
Autores principales: | Jiahai Shi, Nanyu Han, Liangzhong Lim, Shixiong Lua, J Sivaraman, Lushan Wang, Yuguang Mu, Jianxing Song |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2011
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Materias: | |
Acceso en línea: | https://doaj.org/article/f026559c58b04c01ab9e1e26e0f6eea6 |
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