[HTML][HTML] Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibα complex reveals conformation differences with a complex bearing von Willebrand …
JJ Dumas, R Kumar, T McDonagh, F Sullivan… - Journal of Biological …, 2004 - ASBMB
The adhesion of platelets to the subendothelium of blood vessels at sites of vascular injury
under high shear conditions is mediated by a direct interaction between the platelet receptor
glycoprotein Ibα (GpIbα) and the A1 domain of the von Willebrand factor (VWF). Here we
report the 2.6-Å crystal structure of a complex comprised of the extracellular domain of
GpIbα and the wild-type A1 domain of VWF. A direct comparison of this structure to a GpIbα-
A1 complex containing" gain-of-function" mutations, A1-R543Q and GpIbα-M239V, reveals …
under high shear conditions is mediated by a direct interaction between the platelet receptor
glycoprotein Ibα (GpIbα) and the A1 domain of the von Willebrand factor (VWF). Here we
report the 2.6-Å crystal structure of a complex comprised of the extracellular domain of
GpIbα and the wild-type A1 domain of VWF. A direct comparison of this structure to a GpIbα-
A1 complex containing" gain-of-function" mutations, A1-R543Q and GpIbα-M239V, reveals …