Cargando…
Structure of the SARS coronavirus main proteinase as an active C(2) crystallographic dimer
The 34 kDa main proteinase (M(pro)) from the severe acute respiratory syndrome coronavirus (SARS-CoV) plays an important role in the virus life cycle through the specific processing of viral polyproteins. As such, SARS-CoV M(pro) is a key target for the identification of specific inhibitors directed...
Autores principales: | Xu, Ting, Ooi, Amy, Lee, Hooi Chen, Wilmouth, Rupert, Liu, Ding Xiang, Lescar, Julien |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2005
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1978130/ https://www.ncbi.nlm.nih.gov/pubmed/16511208 http://dx.doi.org/10.1107/S1744309105033257 |
Ejemplares similares
-
Mutation of Gly-11 on the Dimer Interface Results in the Complete Crystallographic Dimer Dissociation of Severe Acute Respiratory Syndrome Coronavirus 3C-like Protease: CRYSTAL STRUCTURE WITH MOLECULAR DYNAMICS SIMULATIONS
por: Chen, Shuai, et al.
Publicado: (2008) -
Mutation of Glu-166 Blocks the Substrate-Induced Dimerization of SARS Coronavirus Main Protease
por: Cheng, Shu-Chun, et al.
Publicado: (2010) -
Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase N Terminus Is Indispensable for Proteolytic Activity but Not for Enzyme Dimerization: BIOCHEMICAL AND THERMODYNAMIC INVESTIGATION IN CONJUNCTION WITH MOLECULAR DYNAMICS SIMULATIONS
por: Chen, Shuai, et al.
Publicado: (2005) -
Enzymatic activity of the SARS coronavirus main proteinase dimer
por: Graziano, Vito, et al.
Publicado: (2006) -
C-terminal domain of SARS-CoV main protease can form a 3D domain-swapped dimer
por: Zhong, Nan, et al.
Publicado: (2009)