Integrin αIIbβ3 (platelet GPllb-Illa) binds fibrinogen via recognition sequences such as Arg-Gly-Asp (RGD). Fibrinogen binding requires agonist activation of platelets, whereas the binding of short synthetic RGD peptides does not. We now find that RGD peptide binding leads to changes in αIIbβ3 that are associated with acquisition of high affinity fibrinogen-binding function (activation) and subsequent platelet aggregation. The structural specificities for peptide activation and for inhibition of ligand binding are similar, indicating that both are consequences of occupancy of the same site(s) on αIIbβ3 Thus, the RGD sequence is a trigger of high affinity ligand binding to αIIbβ3 and certain RGD-mimetics are partial agonists as well as competitive antagonists of integrin function.
|Original language||English (US)|
|Number of pages||8|
|State||Published - May 3 1991|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)