Structure and Function of the Von Willebrand Factor A1 Domain

Title: Structure and Function of the Von Willebrand Factor A1 Domain

Volume: 3 Issue: 3

Author(s): Kottayil I. Varughese, Reha Celikel and Zaverio M. Ruggeri

Affiliation:

Keywords: vwf, pro-vwf, vwf a1, gp 1b

Abstract: The role of von Willebrand factor (VWF) in blocking hemorrhage is centered on its ability to act as a bridging adhesive molecule between platelets and components of the extracellular matrix or other platelets. In the course of chronic vascular diseases, moreover, the same properties of VWF may become the cause of pathological thrombus formation leading to arterial occlusion. There is convincing evidence that VWF functions involving interactions with platelets ultimately depend on binding to the membrane glycoprotein (GP) Ibα receptor mediated by the A1 domain. In this review, we present the current knowledge on the structural features of the VWF A1 domain that support its functions.

Cite this article as:

Varughese I. Kottayil, Celikel Reha and Ruggeri M. Zaverio, Structure and Function of the Von Willebrand Factor A1 Domain, Current Protein & Peptide Science 2002; 3 (3) . https://dx.doi.org/10.2174/1389203023380620

DOI https://dx.doi.org/10.2174/1389203023380620	Print ISSN 1389-2037
Publisher Name Bentham Science Publisher	Online ISSN 1875-5550