Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site
(2007) Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology —
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- Abstract
- A series of non-covalent inhibitors of the serine protease dipeptidyl peptidase IV (DPP-IV) were found to adopt a U-shaped binding conformation in X-ray co-crystallization studies. Remarkably, Tyr547 undergoes a 70 degrees side-chain rotation to accommodate the inhibitor and allows access to a previously unexposed area of the protein backbone for hydrogen bonding. (c) 2007 Elsevier Ltd. All rights reserved.
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Sheehan, S. M., Mest, H.-J., Watson, B. M., Klimkowski, V. J., Timm, D. E., Cauvin, A., Parsons, S. H., Shi, Q., Canada, E. J., Wiley, M. R., Ruehter, G., Evers, B., Petersen, S., Blaszczak, L. C., Pulley, S. R., Margolis, B. J., Wishart, G. N., Renson, B., Hankotius, D., et al. (2007). Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site. Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology. https://doi.org/10.1016/j.bmcl.2006.12.074