[HTML][HTML] Critical residues of integrin αIIb subunit for binding of αIIbβ3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3)
T Kamata, A Irie, M Tokuhira, Y Takada - Journal of Biological Chemistry, 1996 - ASBMB
Integrin αIIbβ3 plays a critical role in platelet aggregation through its interaction with
fibrinogen. Elucidation of the mechanisms of αIIbβ3-fibrinogen interaction is critical to
understanding hemostasis and thrombosis. Here we report that mutations of Gly-184, Tyr-
189, Tyr-190, Phe-191, and Gly-193 within the predicted turn structure of the third amino-
terminal repeat of αIIb significantly block binding of αIIbβ3 to soluble fibrinogen. These
mutations also block binding of αIIbβ3 to ligand-mimetic monoclonal antibodies PAC-1, OP …
fibrinogen. Elucidation of the mechanisms of αIIbβ3-fibrinogen interaction is critical to
understanding hemostasis and thrombosis. Here we report that mutations of Gly-184, Tyr-
189, Tyr-190, Phe-191, and Gly-193 within the predicted turn structure of the third amino-
terminal repeat of αIIb significantly block binding of αIIbβ3 to soluble fibrinogen. These
mutations also block binding of αIIbβ3 to ligand-mimetic monoclonal antibodies PAC-1, OP …