Nature Structural Biology
4, 109 - 111 (1997)
doi:10.1038/nsb0297-109
Crystal structure of human osteoclast cathepsin K complex with E-64Baoguang Zhao1, Cheryl A. Janson2, Bernard Y. Amegadzie3, Karla D'Alessio2, Charles Griffin2, Charles R. Hanning3, Christopher Jones2, Jeff Kurdyla2, Michael McQueney2, Xiayang Qiu1, Ward W. Smith1
& Sherin S. Abdel-Meguid1, 4
1Department of Macromolecular Sciences, SmithKline Beecham Pharmaceuticals, 709 Swedeland Road, King of Prussia, Pennsylvania 19406, USA
2Department of Protein Biochemistry, SmithKline Beecham Pharmaceutical, 709 Swedeland Road, King of Prussia, Pennsylvania 19406, USA
3Department of Gene Expression Sciences, SmithKline Beecham Pharmaceutical, 709 Swedeland Road, King of Prussia, Pennsylvania 19406, USA
4sherin_s_abdel-meguid@sbphrd.com The structure of human cathepsin K, a potential target for treatment of osteoporosis, reveals active site differences with homologous cysteine proteinases that should enable the design of cathepsin K selective inhibitors.
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