Key result
The PAR1 hirudin-like sequence reduces kinetic barriers to form the docked thrombin-PAR1 complex and allosterically enhances rapid peptide bond cleavage.
Population
Soluble PAR1 N-terminal exodomains (in vitro biochemical model)
Design
Preclinical
Authors
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No immediate clinical impact; extends kinetic model of thrombin-PAR1 interaction but leaves translation to humans open.
The PAR1 hirudin-like sequence facilitates thrombin docking by reducing kinetic barriers and allosterically enhances receptor cleavage, providing mechanistic insights into platelet activation.
Jacques et al. (2000) studied Platelet activation and aggregation. Soluble PAR1 N-terminal exodomains was evaluated on Mechanism of thrombin-PAR1 recognition and cleavage. The PAR1 hirudin-like sequence reduces kinetic barriers to form the docked thrombin-PAR1 complex and allosterically enhances rapid peptide bond cleavage.
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