作者: E. G. Huizinga
关键词:
摘要: Transient interactions of platelet-receptor glycoprotein Ibalpha (GpIbalpha) and the plasma protein von Willebrand factor (VWF) reduce platelet velocity at sites vascular damage play a role in haemostasis thrombosis. Here we present structures GpIbalpha amino-terminal domain its complex with VWF A1. In complex, wraps around one side A1, providing two contact areas bridged by an area solvated charge interaction. The explain effects gain-of-function mutations related to bleeding disorders provide model for shear-induced activation. These detailed insights into initial adhesion are relevant development antithrombotic drugs.