| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1379390 | Bioorganic & Medicinal Chemistry Letters | 2005 | 5 Pages |
Abstract
The activated Factor VII/tissue factor complex (FVIIa/TF) plays a key role in the formation of blood clots. Inhibition of this complex may lead to new antithrombotic drugs. An X-ray crystal structure of a fluoropyridine-based FVIIa/TF inhibitor bound in the active site of the enzyme complex suggested that incorporation of substitution at the 5-position of the hydroxybenzoic acid side chain could lead to the formation of more potent inhibitors through interactions with the S1′/S2′ pocket.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Jeffrey T. Kohrt, Kevin J. Filipski, Wayne L. Cody, Cuiman Cai, Danette A. Dudley, Chad A. Van Huis, J. Adam Willardsen, Stephen T. Rapundalo, Kamlai Saiya-Cork, Robert J. Leadley, Lakshmi Narasimhan, Erli Zhang, Marc Whitlow, Marc Adler, Kirk McLean,