File:5tdi cathepsinK odanacatib.png

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The X-ray crystallography structure of human cathepsin K in complex with the covalent inhibitor odanacatib, shown in light blue with covalently modified catalytic cysteine in green. Odanacatib was studied in clinical trials as a cathepsin K inhibitor for osteoporosis. Rendered with PyMol from PDB: 5TDI​.

Identification of mouse cathepsin K structural elements that regulate the potency of odanacatib. Law, S., Andrault, P.M., Aguda, A.H., Nguyen, N.T., Kruglyak, N., Brayer, G.D., Bromme, D. (2017) Biochem J 474: 851-864

PubMed: 28049758

DOI: 10.1042/BCJ20160985
Date 27 Deecember 2021
Source Own work
Author Opabinia regalis

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current06:35, 28 December 2021Thumbnail for version as of 06:35, 28 December 2021800 × 600 (266 KB)Opabinia regalis (talk | contribs){{Information |Description=The X-ray crystallography structure of human cathepsin K in complex with the covalent inhibitor odanacatib, shown in light blue with covalently modified catalytic cysteine in green. Odanacatib was studied in clinical trials as a cathepsin K inhibitor for osteoporosis. Rendered with PyMol from {{PDB|5TDI}}. Identification of mouse cathepsin K structural elements that regulate the potency of odanacatib. Law, S., Andrault, P.M., Aguda, A.H., Nguyen, N.T., Kruglyak, N....

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