Figure 1

Potential intradomain interaction of vWF. Partial structure of pro-vWF is shown from vWFpp to vWF A3 domain. ①vWFpp binding to the D’D3 domain of mature vWF occurs in the circulation and attenuates platelet adhesion and activation. ②The D’D3 domain of von Willebrand factor shields the A1 domain in its resting conformation and negatively regulates the binding of A1 domain to GPIb. ③N-terminal flanking region of A1 domain (amino acids Gln1238-Glu1260) in von Willebrand factor stabilizes the structure of A1A2A3 complex and modulates platelet activation under shear stress. ④The recombinant A2 domain of von Willebrand factor specifically binds to the active conformation of A1 domain and blocks the interaction with GPIb.