[HTML][HTML] Shielding of the A1 domain by the D′ D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V
H Ulrichts, M Udvardy, PJ Lenting, I Pareyn… - Journal of Biological …, 2006 - ASBMB
Soluble von Willebrand factor (VWF) has a low affinity for platelet glycoprotein (GP) Ibα and
needs immobilization and/or high shear stress to enable binding of its A1 domain to the
receptor. The previously described anti-VWF monoclonal antibody 1C1E7 enhances
VWF/GPIbα binding and recognizes an epitope in the amino acids 764–1035 region in the N-
terminal D′ D3 domains. In this study we demonstrated that the D′ D3 region negatively
modulates the VWF/GPIb-IX-V interaction;(i) deletion of the D′ D3 region in VWF …
needs immobilization and/or high shear stress to enable binding of its A1 domain to the
receptor. The previously described anti-VWF monoclonal antibody 1C1E7 enhances
VWF/GPIbα binding and recognizes an epitope in the amino acids 764–1035 region in the N-
terminal D′ D3 domains. In this study we demonstrated that the D′ D3 region negatively
modulates the VWF/GPIb-IX-V interaction;(i) deletion of the D′ D3 region in VWF …
