von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule
作者： Zaverio M. Ruggeri , Kottayil I. Varughese , Reha Celikel
DOI: 10.1038/79639
关键词: Von Willebrand factor 、 Platelet 、 Peptide 、 Hemostasis 、 Von Willebrand factor type C domain 、 Biochemistry 、 Methyl group 、 Glycoprotein 、 Chemistry 、 Thrombus 、 Biophysics
摘要: Platelet participation in hemostasis and arterial thrombosis requires the binding of glycoprotein (GP) Ibα to von Willebrand factor (vWF). Hemodynamic forces enhance this interaction, an effect mimicked by substitution I546V vWF A1 domain. A water molecule becomes internalized near deleted Ile methyl group. The change hydrophobicity local environment causes positional changes propagated over a distance 27 A. As consequence, major reorientation peptide plane occurs surface loop involved GP binding. This distinct conformation shows increased platelet adhesion provides structural model for initial regulation thrombus formation.
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