Sandbox Reserved 1447

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Function

The von Willebrand Factor (VWF) plays an important role in stopping the flow of blood, haemostasis. The VWF interacts with functional domains, the vascular wall, coagulation factor VIII, and platelet receptors. When there is a location of vascular injury, the VWF binds to platelets and delivers the coagulation factor VIII to that location of the injury.

Structure

It contains four domains from A-D. The A and B domains contain 3 different domains and C has two domains while D has four. Each domain plays a role in different functions. For example, domains D’ and D3 exhibit binding sites for factor VIII. The structure of VWF was changed from the original thought structure in 1986. The original structure showed to be: D1-D2-D’-D3-A1-A2-A3-D4-B1-B2-B3-C1-C2-CK. However, the new shows the structure is D1-D2-D’-D3-A1-A2-A3-D4-C1-C2-C3-C4-C5-C6-CK. The domain of VWF is the binding site for glycoprotein Ib alpha and for collagen. The A2 domain is responsible for binding the cleavage site to ADAMTS-13. ADAMTS-13 is a metalloprotease that cleaves the VWF.

Disease

As VWF plays a role in coagulation, defects in the VWF leads to a bleeding disorder called von Willebrand Disease that affects 0.01%-1% of the population. 

Structural highlights

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