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Updated: Sep 23, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
Published on: June 3, 2014
Conformation of a bound inhibitor of blood coagulant factor Xa
Daniel R Studelska1, Lynda M McDowell, Marc Adler
1Department of Chemistry, Washington University, St. Louis, Missouri 63130, USA.
Abstract:
13C[(15)N] and (13)C[(19)F] rotational-echo double-resonance NMR have been used to characterize the enzyme-bound structure of ZK-816042, an amidine-imidazoline inhibitor of human factor Xa (FXa). The NMR experiments were performed on a lyophilized FXa-inhibitor complex. The complex was formed in solution in the presence of stabilizing excipients and frozen after gradual supercooling prior to lyophilization. The results indicate that the inhibitor binds with a distribution of orientations of the imidazoline ring.
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