Conformation of a Bound Inhibitor of Blood Coagulant Factor Xa

Abstract
13C{15N} and 13C{19F} 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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