Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1376308 | Bioorganic & Medicinal Chemistry Letters | 2007 | 4 Pages |
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° side-chain rotation to accommodate the inhibitor and allows access to a previously unexposed area of the protein backbone for hydrogen bonding.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Scott M. Sheehan, Hans-Juergen Mest, Brian M. Watson, Valentine J. Klimkowski, David E. Timm, Annick Cauvin, Stephen H. Parsons, Qing Shi, Emily J. Canada, Michael R. Wiley, Gerd Ruehter, Britta Evers, Soenke Petersen, Larry C. Blaszczak, Shon R. Pulley,