The Cytoplasmic Domain of αIIbβ3: A TERNARY COMPLEX OF THE INTEGRIN α AND β SUBUNITS AND A DIVALENT CATION (∗)
TA Haas, EF Plow - Journal of Biological Chemistry, 1996 - ASBMB
Peptides corresponding to the cytoplasmic tails of the α IIb (α IIb (985-1008)) and β 3 (β 3
(713-762)) subunits of the integrin receptor α IIb β 3 (glycoprotein IIb-IIIa) were synthesized
and used to characterize their interaction with cations and with one another. α IIb (985-1008)
was found to contain a functional cation binding site as assessed by both terbium
luminescence and electrospray ionization mass spectroscopy. The binding of Tb 3+ to α IIb
(985-1008) was of high affinity (K d= 8.8±5.2 nM), occurred with a 1: 1 stoichiometry, and …
(713-762)) subunits of the integrin receptor α IIb β 3 (glycoprotein IIb-IIIa) were synthesized
and used to characterize their interaction with cations and with one another. α IIb (985-1008)
was found to contain a functional cation binding site as assessed by both terbium
luminescence and electrospray ionization mass spectroscopy. The binding of Tb 3+ to α IIb
(985-1008) was of high affinity (K d= 8.8±5.2 nM), occurred with a 1: 1 stoichiometry, and …
