Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility.

Abstract

A key regulatory step for serine proteases of the trypsin clan is activation of the initially secreted zymogens, leading to an increase in activity by orders of magnitude. Zymogen activation occurs by cleavage of a single peptide bond near the N-terminus of the catalytic domain. Besides the catalytic domain, most serine proteases have N-terminal A-chains… (More)
DOI: 10.1016/j.jmb.2011.05.026

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@article{Behrens2011ActivationOT, title={Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility.}, author={Manja Annette Behrens and Kenneth A. Botkjaer and Sumit Goswami and Cristiano Luis Pinto Oliveira and Jan K Jensen and Christine R Schar and Paul J Declerck and Cynthia B. Peterson and Peter Andreasen and Jan Skov Pedersen}, journal={Journal of molecular biology}, year={2011}, volume={411 2}, pages={417-29} }