Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine

A potent hepatitis C virus protease protein inhibitor forms an irreversible covalent bond to a virally conserved noncatalytic cysteine in the protease substrate-binding pocket identified in a bioinformatic analysis. Designing selective inhibitors of proteases has proven problematic, in part because...

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Veröffentlicht in:	Nature chemical biology 2011-01, Vol.7 (1), p.22-24
Hauptverfasser:	Hagel, Margit, Niu, Deqiang, St Martin, Thia, Sheets, Michael P, Qiao, Lixin, Bernard, Hugues, Karp, Russell M, Zhu, Zhendong, Labenski, Matthew T, Chaturvedi, Prasoon, Nacht, Mariana, Westlin, William F, Petter, Russell C, Singh, Juswinder
Format:	Artikel
Sprache:	eng
Schlagworte:	631/154/309/2420 631/92/607/468 Biocatalysis Biochemical Engineering Biochemistry Biochemistry - methods Bioorganic Chemistry brief-communication Catalysis Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Crystallography, X-Ray Cysteine - antagonists & inhibitors Cysteine - metabolism Cysteine Proteinase Inhibitors - chemistry Cysteine Proteinase Inhibitors - pharmacology Cysteine Proteinase Inhibitors - therapeutic use Drug Design Hepacivirus - drug effects Hepacivirus - enzymology Hepacivirus - growth & development Oligopeptides - chemistry Oligopeptides - pharmacology Oligopeptides - therapeutic use Pharmacology Protease inhibitors Proteinase inhibitors Proteins Virology - methods
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