ADAMTS‐13 and von Willebrand factor: a dynamic duo

VWF is a key player in haemostasis, acting as a carrier for FVIII and capturing platelets at sites of vascular damage. To capture platelets, it must undergo conformational changes, both within its A1 domain and at the macromolecular level through A2 domain unfolding. Its size and this function are regulated by the metalloproteinase, ADAMTS13. Recently, it has been shown that ADAMTS13 undergoes a conformational change upon interaction with VWF and that this enhances its activity towards its substrate. This review summarises recent work on these conformational transitions, describing how they are controlled. It points to their importance in haemostasis, bleeding disorders and in the developing field of therapeutic application of ADAMTS13 as an antithrombotic agent in obstructive microvascular thrombosis and in cardiovascular disease. This article is protected by copyright. All rights reserved.