Plasticity in interactions of fibroblast growth factor 1 (FGF1) N terminus with FGF receptors underlies promiscuity of FGF1.

@article{Beenken2012PlasticityII,
  title={Plasticity in interactions of fibroblast growth factor 1 (FGF1) N terminus with FGF receptors underlies promiscuity of FGF1.},
  author={Andrew Beenken and Anna V. Eliseenkova and Omar A. Ibrahimi and Shaun K Olsen and Moosa Mohammadi},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 5},
  pages={3067-78}
}
Tissue-specific alternative splicing in the second half of Ig-like domain 3 (D3) of fibroblast growth factor receptors 1-3 (FGFR1 to -3) generates epithelial FGFR1b-FGFR3b and mesenchymal FGFR1c-FGFR3c splice isoforms. This splicing event establishes a selectivity filter to restrict the ligand binding specificity of FGFRb and FGFRc isoforms to mesenchymally and epithelially derived fibroblast growth factors (FGFs), respectively. FGF1 is termed the "universal FGFR ligand" because it overrides… CONTINUE READING

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N-terminal Plasticity Underlies FGF1 Promiscuity

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