ASP514 within the A1 domain of bovine von Willebrand factor is required for interaction with platelet glycoprotein Ib.
A mutant PAD-1 (D514-->Q) of the recombinant fragment PAD-1 comprising Leu469-Ser723 of the A1 domain of bovine von Willebrand factor (vWF) neither inhibited the binding of [125I]vWF to platelets nor the agglutination of human platelets induced by bovine vWF. PAD-1, on the other hand, inhibited human platelet agglutination induced by bovine vWF and [125I]vWF binding to human platelets. Collagen binding properties of the mutant, however, were indistinguishable from those of PAD-1. These results suggested that Asp514 within the A1 domain of vWF is required for interaction of bovine vWF with GPIb receptor on human platelets.
Sinha
D
D
Department of Biochemistry, Temple University School of Medicine, Philadelphia, PA.
Bakhshi
M
M
Kunapuli
S
S
Vora
R
R
Gabriel
J L
JL
Kirby
E P
EP
Budzynski
A Z
AZ
D000818:Animals; D001224:Aspartic Acid; D001665:Binding Sites; D002417:Cattle; D003094:Collagen / Q000378:metabolism; D003198:Computer Simulation; D004563:Electrochemistry; D008958:Models, Molecular; D016296:Mutagenesis; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism*; D017354:Point Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D014841:von Willebrand Factor / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D010980:Platelet Membrane Glycoproteins; D011994:Recombinant Proteins; D014841:von Willebrand Factor; D001224:Aspartic Acid; D003094:Collagen