| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1375906 | Bioorganic & Medicinal Chemistry Letters | 2009 | 4 Pages |
Abstract
A small molecule inhibitor of β-secretase with a unique binding mode has been developed. Crystallographic determination of the enzyme–inhibitor complex shows the catalytic aspartate residues in the active site are not engaged in inhibitor binding. This unprecedented binding mode in the field of aspartyl protease inhibition is described.
Graphical abstractThe unique binding of 5 in the BACE1 active site without catalytic aspartate engagement is described.Figure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Thomas G. Steele, Ivory D. Hills, Ashley A. Nomland, Pablo de León, Timothy Allison, Georgia McGaughey, Dennis Colussi, Katherine Tugusheva, Sharie J. Haugabook, Amy S. Espeseth, Paul Zuck, Samuel L. Graham, Shawn J. Stachel,