Download MendeleyCrystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding.
Huizinga, E.G., Martijn van der Plas, R., Kroon, J., Sixma, J.J., Gros, P.(1997) Structure 5: 1147-1156
- PubMed: 9331419
- DOI: https://doi.org/10.1016/s0969-2126(97)00266-9
- Primary Citation of Related Structures:
1ATZ - PubMed Abstract:
Bleeding from a damaged blood vessel is stopped by the formation of a platelet plug. The multimeric plasma glycoprotein, von Willebrand factor (vWF), plays an essential role in this process by anchoring blood platelets to the damaged vessel wall under conditions of high shear stress. This factor mediates platelet adhesion by binding both to collagen of the damaged blood vessel and to glycoprotein Ib on the platelet membrane. The A3 domain of vWF allows it to bind to collagen types I and III present in the perivascular connective tissue of the damaged vessel wall. To gain insight into the mechanism of collagen binding by vWF, we have determined the crystal structure of the human vWF A3 domain.
Organizational Affiliation:
Department of Haematology, University Hospital Utrecht, The Netherlands.
