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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Veröffentlicht in:Journal of synchrotron radiation. - 1994. - 15(2008), Pt 3 vom: 07. Mai, Seite 204-7
1. Verfasser: Madison, Vincent (VerfasserIn)
Weitere Verfasser: Prongay, Andrew J, Guo, Zhuyan, Yao, Nanhua, Pichardo, John, Fischmann, Thierry, Strickland, Corey, Myers, Joseph Jr, 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
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Journal of synchrotron radiation
Schlagworte:Journal Article NS3 protein, hepatitis C virus NS4A protein, flavivirus Protease Inhibitors Viral Nonstructural Proteins N-(3-amino-1-(cyclobutylmethyl)-2,3-dioxopropyl)-3-(2-((((1,1-dimethylethyl)amino)carbonyl)amino)-3,3-dimethyl-1-oxobutyl)-6,6-dimethyl-3-azabicyclo(3.1.0)hexan-2-carboxamide 89BT58KELH Proline 9DLQ4CIU6V