Cargando…
Crystal Structures Reveal an Induced-fit Binding of a Substrate-like Aza-peptide Epoxide to SARS Coronavirus Main Peptidase
The SARS coronavirus main peptidase (SARS-CoV M(pro)) plays an essential role in the life-cycle of the virus and is a primary target for the development of anti-SARS agents. Here, we report the crystal structure of M(pro) at a resolution of 1.82 Å, in space group P2(1) at pH 6.0. In contrast to the...
Autores principales: | Lee, Ting-Wai, Cherney, Maia M., Liu, Jie, James, Karen Ellis, Powers, James C., Eltis, Lindsay D., James, Michael N.G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Ltd.
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094323/ https://www.ncbi.nlm.nih.gov/pubmed/17196984 http://dx.doi.org/10.1016/j.jmb.2006.11.078 |
Ejemplares similares
-
Crystal Structures of the Main Peptidase from the SARS Coronavirus Inhibited by a Substrate-like Aza-peptide Epoxide
por: Lee, Ting-Wai, et al.
Publicado: (2005) -
A Mechanistic View of Enzyme Inhibition and Peptide Hydrolysis in the Active Site of the SARS-CoV 3C-like Peptidase
por: Yin, Jiang, et al.
Publicado: (2007) -
High-Throughput Screening Identifies Inhibitors of the SARS Coronavirus Main Proteinase
por: Blanchard, Jan E., et al.
Publicado: (2004) -
An Episulfide Cation (Thiiranium Ring) Trapped in the Active Site of HAV 3C Proteinase Inactivated by Peptide-based Ketone Inhibitors
por: Yin, Jiang, et al.
Publicado: (2006) -
The crystal structure of mycobacterial epoxide hydrolase A
por: Schulz, Eike C., et al.
Publicado: (2020)