Mutation G1629E Increases von Willebrand Factor Cleavage via a Cooperative Destabilization Mechanism.

Abstract excerpt

The large multimeric glycoprotein von Willebrand Factor (VWF) plays a pivotal adhesive role during primary hemostasis. VWF is cleaved by the protease ADAMTS13 as a down-regulatory mechanism to prevent excessive VWF-mediated platelet aggregation. For each VWF monomer, the ADAMTS13 cleavage site is located deeply buried inside the VWF A2 domain. External forces in vivo or denaturants in vitro trigger the unfolding...

Topics

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• Proteolysis
• von Willebrand Factor
• ADAMTS13 Protein
• Molecular Dynamics Simulation
• Protein Domains