Abstract
The urokinase-type Plasminogen Activator (uPA) catalyzes the rate limiting step of fibrinolysis, the process by which blood clots are dissolved. This protein has three domains: an EGF-like, a Kringle and a Serine-protease domain. The first two constitute the N-terminal fragment (ATF) which is connected to the serine-protease domain through a disordered linker. Our lab previously showed that the ATF increases the protease activity of uPA towards its substrate Plasminogen by 6-fold. It also reduces the dynamics of the protease domain.
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