Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity.

@article{Olsen2004InsightsIT,
  title={Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity.},
  author={Shaun K. Olsen and Omar A. Ibrahimi and Angela Raucci and Fuming Zhang and Anna V Eliseenkova and Avner Yayon and Claudio Basilico and Robert J. Linhardt and Joseph Schlessinger and Moosa Mohammadi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 4},
  pages={935-40}
}
The prototypical fibroblast growth factor receptor (FGFR) extracellular domain consists of three Ig domains (D1-D3) of which the two membrane-proximal D2 and D3 domains and the interconnecting D2-D3 linker bear the determinants of ligand binding and specificity. In contrast, D1 and the D1-D2 linker are thought to play autoinhibitory roles in FGFR regulation. Here, we report the crystal structure of the three-Ig form of FGFR3c in complex with FGF1, an FGF that binds promiscuously to each of the… CONTINUE READING