Binding interaction of the heregulinbeta egf domain with ErbB3 and ErbB4 receptors assessed by alanine scanning mutagenesis.

@article{Jones1998BindingIO,
  title={Binding interaction of the heregulinbeta egf domain with ErbB3 and ErbB4 receptors assessed by alanine scanning mutagenesis.},
  author={Jennifer T Jones and Marcus D. Ballinger and Paul I. Pisacane and Julie A. Lofgren and Vincent D Fitzpatrick and Wayne J. Fairbrother and James A. Wells and Mark X. Sliwkowski},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 19},
  pages={11667-74}
}
Individual residues of the heregulinbeta (HRG) egf domain were mutated to alanine and displayed monovalently on phagemid particles as gene III fusion proteins. Wild type HRGbeta egf domain displayed on phage was properly folded as evidenced by its ability to bind ErbB3 and ErbB4 receptor-IgG fusion proteins with affinities close to those measured for bacterially produced HRGbeta egf domain. Binding to ErbB3 and ErbB4 receptors was affected by mutation of residues throughout the egf domain… CONTINUE READING

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