Evidence that the intracellular domain of FGF receptor 2IIIb affects contact of the ectodomain with two FGF7 ligands.

@article{Uematsu2001EvidenceTT,
  title={Evidence that the intracellular domain of FGF receptor 2IIIb affects contact of the ectodomain with two FGF7 ligands.},
  author={Fumiyuki Uematsu and Jun Hyeog Jang and Mirjam van Kan and Fang Wang and Yongzhang Luo and Wallace L. Mckeehan},
  journal={Biochemical and biophysical research communications},
  year={2001},
  volume={283 4},
  pages={791-7}
}
Models of the oligomeric FGF signaling complex, including those derived from crystal structures, vary in stoichiometry and arrangement of the three subunits comprised of heparin/heparan sulfate chains, FGFR tyrosine kinase and activating FGF. Here, using covalent affinity crosslinking of radiolabeled FGF7 to binary complexes of FGFR2IIIb and heparin, we show that two molecules of FGF7 contact each FGFR2IIIb. This supports models that propose a dimeric complex of two units with stoichiometry 1… CONTINUE READING