German Scientists investigate the structure of the von Willebrand factor (VWF), a key protein involved in blood clotting. HITS researchers from the Molecular Biomechanics group simulated the dynamics of the platelet integrin-binding VWF C4 domain to better understand disease mutations of this protein. The project was supported by the Deutsche Forschungsgemeinschaft (DFG).
The von Willebrand factor (VWF) protein is a key player in the regulation of haemostasis, i.e. blood clotting. It binds to proteins on the surface of blood platelets, thus assisting the process of platelet aggregation which causes a blood clot to form. Since 2011, a group of researchers funded by the Deutsche Forschungsgemeinschaft (http://www.shenc.de/ ) have been investigating the structure and the function of this important protein. In a new paper published in the journal Blood, they report the structure of a key region of VWF known as the C4 domain. In this study, HITS researcher Prof. Frauke Gräter (Molecular Biomechanics group) and her colleagues Dr. Camilo Aponte-Santamaria and Dr. Katra Kolsek simulated a key region of the protein, called C4 domain. In conjunction with experimental measurements, they jointly with colleagues at EMBL revealed the dynamics of this region at atomistic detail, which might help in future to better understand how VWF-related diseases come about.
Interview with project partners Matthias Wilmanns and Janosch Hennig (both EMBL Heidelberg): https://news.embl.de/science/new-insights-into-the-regulation-of-haemostasis/