Analysis of high-affinity binding determinants in the receptor binding epitope of basic fibroblast growth factor.

@article{Zhu1997AnalysisOH,
  title={Analysis of high-affinity binding determinants in the receptor binding epitope of basic fibroblast growth factor.},
  author={H Zhu and Jerry M. Anchin and K. Ramnarayan and Jie Zheng and Toshihisa Kawai and S J Mong and Manfred E. Wolff},
  journal={Protein engineering},
  year={1997},
  volume={10 4},
  pages={417-21}
}
Basic fibroblast growth factor (bFGF) is implicated in the pathogenesis of several vascular and connective diseases. A key step in the discovery of bFGF receptor antagonists to mitigate these actions is to define the functional epitope required for receptor binding of the growth factor. In previous studies, we identified Glu96 as an essential residue in this epitope using site-directed mutagenesis. Here we examined the role of solvent accessible neighboring residues of Glu96 of bFGF on receptor… CONTINUE READING

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