Abstract
Von Willebrand factor (VWF) is a large multimeric, multidomain glycoprotein that circulates in the bloodstream and is essential for mediating platelet adhesion at sites of vascular injury through its A1 domain. Our lab has recently provided detailed characterizations of the autoinhibitory module (AIM), the discontinuous flanking regions that cooperatively shield the A1 domain and regulate its binding to cognate platelet receptor glycoprotein (GP) Ibα. While our recent analyses have described the mechanical and biochemical properties of AIM-A1 as an independent functional unit, the impact of the neighboring D’D3 and A2 domains on AIM dynamics remain unclear.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
