SOLUTION STRUCTURE AND AGGREGATION OF VON WILLEBRAND FACTOR STUDIED BY NEUTRON AND LIGHT SCATTERING

2004 ◽  
Vol 13 (3) ◽  
pp. 176
Author(s):  
Sriram Neelamegham ◽  
Harish Shankaran
Keyword(s):  
Light Scattering ◽  
Von Willebrand Factor ◽  
Solution Structure ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Solution Structure of Human von Willebrand Factor Studied Using Small Angle Neutron Scattering

2006 ◽  
Vol 281 (50) ◽  
pp. 38266-38275 ◽  
Author(s):  
Indrajeet Singh ◽  
Harish Shankaran ◽  
Mark E. Beauharnois ◽  
Zhihua Xiao ◽  
Paschalis Alexandridis ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Von Willebrand Factor ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Solution Structure ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Structure and dynamics of the platelet integrin-binding C4 domain of von Willebrand factor

Blood ◽  
2019 ◽  
Vol 133 (4) ◽  
pp. 366-376 ◽  
Author(s):  
Emma-Ruoqi Xu ◽  
Sören von Bülow ◽  
Po-Chia Chen ◽  
Peter J. Lenting ◽  
Katra Kolšek ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Conformational Changes ◽  
Solution Structure ◽  
Disulfide Bridges ◽  
Short Segment ◽  
Structure And Dynamics ◽  
Open Conformation ◽  
Force Activation ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Von Willebrand factor (VWF) is a key player in the regulation of hemostasis by promoting recruitment of platelets to sites of vascular injury. An array of 6 C domains forms the dimeric C-terminal VWF stem. Upon shear force activation, the stem adopts an open conformation allowing the adhesion of VWF to platelets and the vessel wall. To understand the underlying molecular mechanism and associated functional perturbations in disease-related variants, knowledge of high-resolution structures and dynamics of C domains is of paramount interest. Here, we present the solution structure of the VWF C4 domain, which binds to the platelet integrin and is therefore crucial for the VWF function. In the structure, we observed 5 intra- and inter-subdomain disulfide bridges, of which 1 is unique in the C4 domain. The structure further revealed an unusually hinged 2-subdomain arrangement. The hinge is confined to a very short segment around V2547 connecting the 2 subdomains. Together with 2 nearby inter-subdomain disulfide bridges, this hinge induces slow conformational changes and positional alternations of both subdomains with respect to each other. Furthermore, the structure demonstrates that a clinical gain-of-function VWF variant (Y2561) is more likely to have an effect on the arrangement of the C4 domain with neighboring domains rather than impairing platelet integrin binding.

scholarly journals Solution structure of human blood protein Von Willebrand factor

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Sriram Neelamegham ◽  
Indrajeet Singh ◽  
Harish Shankaran
Keyword(s):  
Von Willebrand Factor ◽  
Human Blood ◽  
Solution Structure ◽  
Blood Protein ◽  
Von Willebrand ◽  
Willebrand Factor

Determination of the solution structure of a platelet-adhesion peptide of von Willebrand factor

Biochemistry ◽  
1992 ◽  
Vol 31 (45) ◽  
pp. 11152-11158 ◽  
Author(s):  
Heather M. Knott ◽  
Michael C. Berndt ◽  
Andrew V. Kralicek ◽  
Sean I. O'Donoghue ◽  
Glenn F. King
Keyword(s):  
Von Willebrand Factor ◽  
Solution Structure ◽  
Platelet Adhesion ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Solution Structure and Dynamics of a Prototypical Chordin-like Cysteine-rich Repeat (von Willebrand Factor Type C Module) from Collagen IIA

2004 ◽  
Vol 279 (51) ◽  
pp. 53857-53866 ◽  
Author(s):  
Joanne M. O'Leary ◽  
John M. Hamilton ◽  
Charlotte M. Deane ◽  
Najl V. Valeyev ◽  
Linda J. Sandell ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Solution Structure ◽  
Structure And Dynamics ◽  
Type C ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor
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