Von Willebrand factor type D domain
| VWD | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | VWD | ||||||||
| Pfam | PF00094 | ||||||||
| InterPro | IPR001846 | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
In molecular biology, the protein domain Von Willebrand factor type D domain belongs to a large family of proteins, named, the von Willebrand factor (vWF). These proteins, the vWF type D domain in particular, is a large, multimeric glycoprotein and it is synthesized by a type of bone marrow cell called megakaryocytes. vWF type D plays 2 important roles in stopping the blood flow or loss of blood. Firstly, it causes platelets to adhere to the inside of the damaged blood vessel walls to prevent leakage of blood. Secondly, it is a carrier protein for factor VIII (FVIII) which helps blood to clot.
One of the functions of von Willebrand factor (vWF) is to serve as a carrier of clotting factor VIII (FVIII). The native conformation of the D' domain of vWF is not only required for factor VIII (FVIII) binding but also for normal multimerisation and optimal secretion. The interaction between blood clotting factor VIII and VWF is necessary for normal survival of blood clotting factor VIII in blood circulation. The VWFD domain is a highly structured region, in which the first conserved Cys has been found to form a disulphide bridge with the second conserved one.
The D8 domain (amino acids 6-102) is a highly structured region containing 24 paired cysteine residues. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands.
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