Linker regions and flexibility around the metalloprotease domain account for conformational activation of ADAMTS‐13

Recently, conformational activation of ADAMTS-13 was identified. This mechanism showed the evolution from a condensed conformation, in which the proximal MDTCS and distal T2-CUB2 domains are in close contact with each other, to an activated, open structure due to binding with von Willebrand factor (VWF).Identification of cryptic epitope/exosite exposure after conformational activation and of sites of flexibility in ADAMTS-13.The activating...