| Literature DB >> 16125385 |
Jeffrey T Kohrt1, 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, Yuo-Ling Chou, Cecile McKnight, Damian O Arnaiz, Kenneth J Shaw, David R Light, Jeremy J Edmunds.
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.Entities:
Mesh：
Substances：
Year: 2005 PMID： 16125385 DOI： 10.1016/j.bmcl.2005.07.059
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823