Dynamically-Driven Enhancement of the Catalytic Machinery of the SARS 3C-Like Protease by the S284-T285-I286/A Mutations on the Extra Domain

Previously we revealed that the extra domain of SARS 3CLpro mediated the catalysis via different mechanisms. While the R298A mutation completely abolished the dimerization, thus resulting in the inactive catalytic machinery, N214A inactivated the enzyme by altering its dynamics without significantly...

Descripción completa

Detalles Bibliográficos
Autores principales: Lim, Liangzhong, Shi, Jiahai, Mu, Yuguang, Song, Jianxing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4103764/
https://www.ncbi.nlm.nih.gov/pubmed/25036652
http://dx.doi.org/10.1371/journal.pone.0101941

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4103764/
https://www.ncbi.nlm.nih.gov/pubmed/25036652
http://dx.doi.org/10.1371/journal.pone.0101941

Ejemplares similares