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- W2490271950 abstract "Novel, potent and selective human osteoclast cathepsin K inhibitors have been designed based on knowledge derived from the crystal structure of papain bound to a tripeptide aldehyde. Cathepsin K is a thiol protease belonging to the papain superfamily. Unlike previously known crystal structures of that family of enzymes in which ligands bind to the nonprime side of the active site, our papain structure shows the ligand in the prime direction. This observation and the identification of key interactions between the protein and the ligand inspired the design of a novel class of inhibitors spanning both sides of the active site. The crystal structure of the first member of this class bound to cathepsin K confirmed our design hypothesis. Inhibitors of cathepsin K are potential drugs for the treatment of osteoporosis." @default.
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- W2490271950 date "1999-07-07" @default.
- W2490271950 modified "2023-10-16" @default.
- W2490271950 title "Rational Approaches to Inhibition of Human Osteoclast Cathepsin K and Treatment of Osteoporosis" @default.
- W2490271950 doi "https://doi.org/10.1021/bk-1999-0719.ch009" @default.
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