Cargando…
A computational analysis of SARS cysteine proteinase-octapeptide substrate interaction: implication for structure and active site binding mechanism
BACKGROUND: SARS coronavirus main proteinase (SARS CoVMpro) is an important enzyme for the replication of Severe Acute Respiratory Syndrome virus. The active site region of SARS CoVMpro is divided into 8 subsites. Understanding the binding mode of SARS CoVMpro with a specific substrate is useful and...
Autores principales: | Phakthanakanok, Krongsakda, Ratanakhanokchai, Khanok, Kyu, Khin Lay, Sompornpisut, Pornthep, Watts, Aaron, Pinitglang, Surapong |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2648740/ https://www.ncbi.nlm.nih.gov/pubmed/19208150 http://dx.doi.org/10.1186/1471-2105-10-S1-S48 |
Ejemplares similares
-
Synthesis and activity of an octapeptide inhibitor designed for SARS coronavirus main proteinase
por: Gan, Yi-Ru, et al.
Publicado: (2006) -
Viral cysteine proteinases
por: Gorbalenya, Alexander E., et al.
Publicado: (1996) -
The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase()
por: Wei, Ping, et al.
Publicado: (2006) -
Cysteine proteinases of microorganisms and viruses
por: Rudenskaya, G. N., et al.
Publicado: (2011) -
Exploring polyamine interactions and binding pockets in SARS-CoV-2 ORF3a
por: Boonamnaj, Panisak, et al.
Publicado: (2023)