|PROSITE documentation PDOC50234 [for PROSITE entry PS50234]|
Von Willebrand factor (VWF) is a large, multimeric blood glycoprotein that is required for normal hemostasis. Mutant forms are involved in the most common inherited bleeding disorder (von Willebrand disease: VWD). VWF mediates the adhesion of platelets to sites of vascular damage by binding to specific platelet membrane glycoproteins and to constituents of exposed connective tissue. It is also essential for the transport of the blood clotting factor VIII [1,2].
VWF is a large multidomain protein. Among those domains the type A domain is known to be distributed in at least 22 human proteins, all of them being extracellular. In VWF there is 3 repeats of the type A domain (A1,A2,A3) that have been shown to bind other proteins like collagen and heparin. The 3D structure of A1 and A3 has been published [3,4]. The domain adopts a classic α/β "Rossmann" fold.
The following proteins have been found to contain a VWFA domain:
We developed a profile that spans the whole domain.Last update:
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||Biochemistry and genetics of von Willebrand factor.|
|Source||Annu. Rev. Biochem. 67:395-424(1998).|
|2||Authors||Voorberg J., Fontijn R., van Mourik J.A., Pannekoek H.|
|Title||Domains involved in multimer assembly of von willebrand factor (vWF): multimerization is independent of dimerization.|
|Source||EMBO J. 9:797-803(1990).|
|3||Authors||Huizinga E.G., Martijn van der Plas R., Kroon J., Sixma J.J., Gros P.|
|Title||Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding.|
|4||Authors||Emsley J., Cruz M., Handin R., Liddington R.|
|Title||Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib.|
|Source||J. Biol. Chem. 273:10396-10401(1998).|