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

Characterization of a single-domain von Willebrand factor type C protein (HaSVC) from the salivary gland of the tick Hyalomma asiaticum

2021 ◽  
pp. 108190
Author(s):  
Haiyan Gong ◽  
Jialin Yao ◽  
Bingbing Zhang ◽  
Yongzhi Zhou ◽  
Houshuang Zhang ◽  
...  
Keyword(s):  
Salivary Gland ◽  
Von Willebrand Factor ◽  
Single Domain ◽  
C Protein ◽  
Type C ◽  
Factor Type ◽  
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 Binding between Crossveinless-2 and Chordin Von Willebrand Factor Type C Domains Promotes BMP Signaling by Blocking Chordin Activity

PLoS ONE ◽  
2010 ◽  
Vol 5 (9) ◽  
pp. e12846 ◽  
Author(s):  
Jin-Li Zhang ◽  
Lucy J. Patterson ◽  
Li-Yan Qiu ◽  
Daria Graziussi ◽  
Walter Sebald ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Bmp Signaling ◽  
Type C ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Molecular Characterization of the Von Willebrand Factor Type D Domain of Vitellogenin from Takifugu flavidus

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 181
Author(s):  
Kun Qiao ◽  
Caiyun Jiang ◽  
Min Xu ◽  
Bei Chen ◽  
Wenhui Qiu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Von Willebrand Factor ◽  
Molecular Mechanisms ◽  
Protein Domain ◽  
Type D ◽  
Protein Toxin ◽  
Factor Type ◽  
Von Willebrand ◽  
Willebrand Factor

The von Willebrand factor type D (VWD) domain in vitellogenin has recently been found to bind tetrodotoxin. The way in which this protein domain associates with tetrodotoxin and participates in transporting tetrodotoxin in vivo remains unclear. A cDNA fragment of the vitellogenin gene containing the VWD domain from pufferfish (Takifugu flavidus) (TfVWD) was cloned. Using in silico structural and docking analyses of the predicted protein, we determined that key amino acids (namely, Val115, ASP116, Val117, and Lys122) in TfVWD mediate its binding to tetrodotoxin, which was supported by in vitro surface plasmon resonance analysis. Moreover, incubating recombinant rTfVWD together with tetrodotoxin attenuated its toxicity in vivo, further supporting protein–toxin binding and indicating associated toxicity-neutralizing effects. Finally, the expression profiling of TfVWD across different tissues and developmental stages indicated that its distribution patterns mirrored those of tetrodotoxin, suggesting that TfVWD may be involved in tetrodotoxin transport in pufferfish. For the first time, this study reveals the amino acids that mediate the binding of TfVWD to tetrodotoxin and provides a basis for further exploration of the molecular mechanisms underlying the enrichment and transfer of tetrodotoxin in pufferfish.

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