binding to substrate von Willebrand factor D4 allosterically activates ADAMTS13, increasing its catalytic activity. Binding also positions ADAMTS13 on the substrate where it can act rapidly when shear stress exposes the scissile bond in the adjacent A2 domain
the enzyme is conformationally activated by von Willebrand factor which engages the TSP8-CUB2 domains, inducing the conformational change that disrupts the CUB1-spacer domain interaction and thereby activates the enzyme
Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation
Formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13: a new prothrombotic mechanism in diseases associated with oxidative stress
Lancellotti, S.; De Filippis, V.; Pozzi, N.; Peyvandi, F.; Palla, R.; Rocca, B.; Rutella, S.; Pitocco, D.; Mannucci, P.M.; De Cristofaro, R.