دورية
Use of Papain as a Model for the Structure-Based Design of Cathepsin K Inhibitors: Crystal Structures of Two Papain−Inhibitor Complexes Demonstrate Binding to S-Subsites
العنوان: | Use of Papain as a Model for the Structure-Based Design of Cathepsin K Inhibitors: Crystal Structures of Two Papain−Inhibitor Complexes Demonstrate Binding to S-Subsites |
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المؤلفون: | LaLonde, J. M., Zhao, B., Smith, W. W., Janson, C. A., DesJarlais, R. L., Tomaszek, T. A., Carr, T. J., Thompson, S. K., Oh, H.-J., Yamashita, D. S., Veber, D. F., Abdel-Meguid, S. S. |
المصدر: | Journal of Medicinal Chemistry; November 5, 1998, Vol. 41 Issue: 23 p4567-4576, 10p |
مستخلص: | Papain has been used as a surrogate enzyme in a drug design effort to obtain potent and selective inhibitors of cathepsin K, a new member of the papain superfamily of cysteine proteases that is selectively and highly expressed in osteoclasts and is implicated in bone resorption. Here we report the crystal structures of two papain−inhibitor complexes and the rational design of novel cathepsin K inhibitors. Unlike previously known crystal structures of papain−inhibitor complexes, our papain structures show ligand binding extending deep within the S-subsites. The two inhibitor complexes, carbobenzyloxyleucinyl-leucinyl-leucinal and carbobenzyloxy- |
قاعدة البيانات: | Supplemental Index |
تدمد: | 00222623 15204804 |
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