Characterization of a core binding site for ADAMTS-13 in the A2 domain of von Willebrand factor.

  title={Characterization of a core binding site for ADAMTS-13 in the A2 domain of von Willebrand factor.},
  author={J Wu and Kazuo Fujikawa and Brad A. McMullen and Dominic W Chung},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={103 49},
ADAMTS-13, a metalloprotease in plasma, specifically cleaves the Tyr-1605-Met-1606 bond in the A2 domain of von Willebrand factor (VWF) to regulate the polymer distribution of VWF in circulation, which is critical for primary hemostasis. A 73-aa peptide (VWF73) was previously identified as the minimal substrate cleavable by ADAMTS-13. In this study, VWF73 was enzymatically and chemically cleaved into shorter peptides, and the inhibition of cleavage of a VWF73-derived substrate by these purified… CONTINUE READING
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