Divalent cations differentially regulate integrin αIIb cytoplasmic tail binding to β3 and to calcium-and integrin-binding protein
L Vallar, C Melchior, S Plançon, H Drobecq… - Journal of Biological …, 1999 - ASBMB
We have used recombinant or synthetic α IIb and β 3 integrin cytoplasmic peptides to study
their in vitro complexation and ligand binding capacity by surface plasmon resonance. α· β
heterodimerization occurred in a 1: 1 stoichiometry with a weakK D in the micromolar range.
Divalent cations were not required for this association but stabilized the α· β complex by
decreasing the dissociation rate. α· β complexation was impaired by the R995A substitution
or the KVGFFKR deletion in α IIb but not by the β 3 S752P mutation. Recombinant calcium …
their in vitro complexation and ligand binding capacity by surface plasmon resonance. α· β
heterodimerization occurred in a 1: 1 stoichiometry with a weakK D in the micromolar range.
Divalent cations were not required for this association but stabilized the α· β complex by
decreasing the dissociation rate. α· β complexation was impaired by the R995A substitution
or the KVGFFKR deletion in α IIb but not by the β 3 S752P mutation. Recombinant calcium …