Abstract
PLATELET membrane glycoprotein Ilb-IIIa (gpIIb-IIIa; αllb-β3), the most prominent member of the integrin family of adhesion receptors on these cells, mediates platelet aggregation by binding fibrinogen and is critical in thrombosis and haemostasis1-5. A short amino-acid sequence at the carboxy terminus of the γ chain of fibrinogen is recognized by gpIIb-IIIa (ref. 6) and peptides containing this sequence are selectively crosslinked to residues 294-314 of gpllb (ref. 7). Here we show that an 11-residue peptide from this region of gpllb inhibits platelet aggregation and binding of fibrinogen to platelets and to purified gpIIb-IIIa, and that it interacts directly with fibrinogen. These results implicate this segment of gpIIb-IIIa in the ligand-binding function of the receptor. Moreover, as this region is highly conserved among integrins, it may have a general function in ligand recognition by this broadly distributed family of adhesion receptors.
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D'Souza, S., Ginsberg, M., Matsueda, G. et al. A discrete sequence in a platelet integrin is involved in ligand recognition. Nature 350, 66–68 (1991). https://doi.org/10.1038/350066a0
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DOI: https://doi.org/10.1038/350066a0
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