Divalent cations differentially regulate integrin alphaIIb cytoplasmic tail binding to beta3 and to calcium- and integrin-binding protein.

@article{Vallar1999DivalentCD,
  title={Divalent cations differentially regulate integrin alphaIIb cytoplasmic tail binding to beta3 and to calcium- and integrin-binding protein.},
  author={Laurent Vallar and Chantal Melchior and S{\'e}bastien Plançon and Herv{\'e} Drobecq and Guy Lippens and V{\'e}ronique R{\'e}gnault and Nelly Kieffer},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 24},
  pages={17257-66}
}
We have used recombinant or synthetic alphaIIb and beta3 integrin cytoplasmic peptides to study their in vitro complexation and ligand binding capacity by surface plasmon resonance. alpha.beta heterodimerization occurred in a 1:1 stoichiometry with a weak KD in the micromolar range. Divalent cations were not required for this association but stabilized the alpha.beta complex by decreasing the dissociation rate. alpha.beta complexation was impaired by the R995A substitution or the KVGFFKR… CONTINUE READING

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