Key steps in the structure-based optimization of the hepatitis C virus NS3/4A protease inhibitor SCH503034

The structures of both native and S139A holo-HCV NS3/4A protease domain were solved to high resolution. Subsequently, structures were determined for a series of ketoamide inhibitors in complex with the protease. The changes in the inhibitor potency were correlated with changes in the buried surface...

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Detalles Bibliográficos
Autores principales: Madison, Vincent, Prongay, Andrew J., Guo, Zhuyan, Yao, Nanhua, Pichardo, John, Fischmann, Thierry, Strickland, Corey, Myers Jr, Joseph, Weber, Patricia C., Beyer, Brian M., Ingram, Richard, Hong, Zhi, Prosise, Winifred W., Ramanathan, Lata, Taremi, S. Shane, Yarosh-Tomaine, Taisa, Zhang, Rumin, Senior, Mary, Yang, Rong-Sheng, Malcolm, Bruce, Arasappan, Ashok, Bennett, Frank, Bogen, Stephane L., Chen, Kevin, Jao, Edwin, Liu, Yi-Tsung, Lovey, Raymond G., Saksena, Anil K., Venkatraman, Srikanth, Girijavallabhan, Viyyoor, Njoroge, F. George
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2008
Materias:
Diffraction Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394794/
https://www.ncbi.nlm.nih.gov/pubmed/18421139
http://dx.doi.org/10.1107/S0909049507064229

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394794/
https://www.ncbi.nlm.nih.gov/pubmed/18421139
http://dx.doi.org/10.1107/S0909049507064229

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