Competition for related but nonidentical binding sites on the glycoprotein IIb-IIIa complex by peptides derived from platelet adhesive proteins.

Santoro SA, Lawing WJ
Cell. 1987 48 (5): 867-73

PMID: 3493077 · DOI:10.1016/0092-8674(87)90083-3

Two distinct sequences of amino acids, RGDS and HHLGGAKQAGDV, each inhibit the binding of fibrinogen, fibronectin, and von Willebrand factor to the platelet membrane glycoprotein IIb-IIIa complex. We have employed radiolabeled, photoactivatable aryl azide derivatives of the two sequences to explore the relationship between the binding sites for these peptides on the glycoprotein IIb-IIIa complex. Each probe specifically labeled only the glycoprotein IIb-IIIa complex of intact platelets. Since each peptide inhibited labeling of the receptor complex by the other, the peptides compete for binding sites on the receptor complex. However, the binding sites do not appear to be identical. Whereas the RGDS probe specifically labeled both glycoproteins IIb and IIIa, the HHLGGAKQA-GDV probe specifically labeled only glycoprotein IIb.

MeSH Terms (14)

Amino Acid Sequence Binding, Competitive Binding Sites Blood Platelets Blood Proteins Fibrinogen Fibronectins Humans Kinetics Oligopeptides Peptides Platelet Membrane Glycoproteins Protein Binding von Willebrand Factor

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