Effects of Pro1266Leu mutation on structure and function of glycoprotein Ib binding domain of von Willebrand factor

2019 ◽  
Vol 120 (10) ◽  
pp. 17847-17857 ◽  
Author(s):  
Ahmad Abu Turab Naqvi ◽  
Mohamed F. Alajmi ◽  
Tabish Rehman ◽  
Afzal Hussain ◽  
Imtaiyaz Hassan
Keyword(s):  
Von Willebrand Factor ◽  
Structure And Function ◽  
Binding Domain ◽  
Glycoprotein Ib ◽  
And Function ◽  
Von Willebrand ◽  
Willebrand Factor

Functional modulation of the isolated glycoprotein Ib binding domain of von Willebrand factor expressed in Escherichia coli [Erratum to document cited in CA114(23):226555u]

Biochemistry ◽  
1991 ◽  
Vol 30 (51) ◽  
pp. 11850-11850
Author(s):  
Mitsuhiko Sugimoto ◽  
George Ricca ◽  
Michael E. Hrinda ◽  
Alain B. Schreiber ◽  
George H. Searfoss ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Von Willebrand Factor ◽  
Binding Domain ◽  
Glycoprotein Ib ◽  
Functional Modulation ◽  
Von Willebrand ◽  
Willebrand Factor

Functional modulation of the isolated glycoprotein Ib binding domain of von Willebrand factor expressed in Escherichia coli

Biochemistry ◽  
1991 ◽  
Vol 30 (21) ◽  
pp. 5202-5209 ◽  
Author(s):  
Mitsuhiko Sugimoto ◽  
George Ricca ◽  
Michael E. Hrinda ◽  
Alain B. Schreiber ◽  
George H. Searfoss ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Von Willebrand Factor ◽  
Binding Domain ◽  
Glycoprotein Ib ◽  
Functional Modulation ◽  
Von Willebrand ◽  
Willebrand Factor

Recombinant von Willebrand Factor-Insight into Structure and Function through Infusion Studies in Animals with Severe von Willebrand Disease

2002 ◽  
Vol 28 (2) ◽  
pp. 215-226 ◽  
Author(s):  
Hans Peter Schwarz ◽  
Uwe Schlokat ◽  
Artur Mitterer ◽  
Katalin Váradi ◽  
Herbert Gritsch ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Structure And Function ◽  
Von Willebrand Disease ◽  
And Function ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Insight Into

scholarly journals The binding domain of von Willebrand factor to sulfatides is distinct from those interacting with glycoprotein Ib, heparin, and collagen and resides between amino acid residues Leu 512 and Lys 673

Blood ◽  
1991 ◽  
Vol 78 (9) ◽  
pp. 2310-2317 ◽  
Author(s):  
O Christophe ◽  
B Obert ◽  
D Meyer ◽  
JP Girma
Keyword(s):  
Von Willebrand Factor ◽  
Competitive Inhibition ◽  
Binding Domain ◽  
Functional Site ◽  
Platelet Glycoprotein ◽  
Functional Domain ◽  
Amino Acid Residues ◽  
Glycoprotein Ib ◽  
Von Willebrand ◽  
Willebrand Factor

A series of proteolytic fragments of human von Willebrand Factor (vWF) was purified to characterize the functional site that supports its interaction with sulfatides. SpIII, an N-terminal homodimer generated by V-8 protease (amino acids [AA] 1 to 1365), bound to sulfatides in a dose-dependent and saturable way. SpIII also totally inhibited the binding of vWF to sulfatides and SpIII binding was completely abolished by vWF. In contrast, SpII, the complementary C-terminal homodimer (AA 1366 to 2050), did not exhibit any binding affinity for sulfatides. Four purified fragments overlapping the sequence of SpIII were also tested for their ability to interact with sulfatides. An N-terminal monomeric 34-Kd fragment (P34, AA 1 to 272) generated by plasmin, a central monomer (SpI, AA 911 to 1365) produced by digestion with V-8 protease, and a tetrameric fragment III-T2 (comprising a pair of the two sequences AA 273 to 511 and AA 674 to 728) produced by secondary digestion of SpIII with trypsin did not interact with sulfatides. In contrast, a monomeric 39/34-Kd fragment produced by dispase (AA 480 to 718) bound specifically and with a high affinity to sulfatides and totally displaced vWF or SpIII binding. Conversely, binding of the 39/34-Kd species was totally abolished by vWF or SpIII. Thus, a functional site responsible for sulfatide binding was localized between AA 480 and 718 and comparison of the binding properties of the 39/34-Kd and III-T2 fragments indicated that the sequence 512 to 673 is necessary for the binding to sulfatides. Further mapping of this new functional domain of vWF, based on experiments of competitive inhibition of binding by either heparin or monoclonal antibodies directed toward vWF, showed that the site interacting with sulfatides is distinct from those involved in binding to platelet glycoprotein Ib, collagen, or heparin. This finding was confirmed by experiments using synthetic peptides which also indicated that the sequence comprising AA 569 to 584 is part of the sulfatide-binding domain or influences its activity.

Sign in / Sign up

Export Citation Format

Share Document