Expression and purification of recombinant human fibroblast growth factor receptor in Escherichia coli.

@article{Ryu2006ExpressionAP,
  title={Expression and purification of recombinant human fibroblast growth factor receptor in Escherichia coli.},
  author={Eui Kyung Ryu and Ki Joon Cho and Jin Kwang Kim and Nicholas J Harmer and Tom L. Blundell and Kyung Hyun Kim},
  journal={Protein expression and purification},
  year={2006},
  volume={49 1},
  pages={15-22}
}
Human fibroblast growth factor receptor (FGFR) is responsible for multifunctional signaling that regulates developmental processes. The three immunoglobulin-like extracellular domains of FGFR (D1, D2, and D3) include the determinants of ligand binding and specificity for fibroblast growth factor and heparan sulfate. D1 and the D1-D2 linker with a contiguous stretch of acidic amino acids are known to be involved in auto-inhibitory regulation. In an effort to gain a better understanding of the… CONTINUE READING

Citations

Publications citing this paper.

Similar Papers

Loading similar papers…