¹⁹F NMR reveals the conformational properties of free thrombin and its zymogen precursor prethrombin-2.

ABSTRACT: The conformational properties of trypsin-like proteases and their zymogen forms remain controversial because of a lack of sufficient information on their free forms. Specifically, it is unclear whether the free protease is zymogen-like and shifts to its mature form upon a ligand-induced fit or exists in multiple conformations in equilibrium from which the ligand selects the optimal fit via conformational selection. Here we report the results of ¹⁹F NMR measurements that reveal the conformational properties of a protease and its zymogen precursor in the free form. Using the trypsin-like, clotting protease thrombin as a relevant model system, we show that its conformation is quite different from that of its direct zymogen precursor prethrombin-2 and more similar to that of its ful

SUBMITTER: Ruben EA 

PROVIDER: S-EPMC7294081 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature