Structural and biophysical characterization of the EphB4*ephrinB2 protein-protein interaction and receptor specificity.

@article{Chrencik2006StructuralAB,
  title={Structural and biophysical characterization of the EphB4*ephrinB2 protein-protein interaction and receptor specificity.},
  author={Jill E. Chrencik and Alexei Brooun and Michelle L Kraus and Michael I. Recht and Anand R Kolatkar and Gye Won Han and Jan Seifert and Hans Widmer and Manfred Auer and Peter Kuhn},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 38},
  pages={
          28185-92
        }
}
Increasing evidence implicates the interaction of the EphB4 receptor with its preferred ligand, ephrinB2, in pathological forms of angiogenesis and in tumorigenesis. To identify the molecular determinants of the unique specificity of EphB4 for ephrinB2, we determined the crystal structure of the ligand binding domain of EphB4 in complex with the extracellular domain of ephrinB2. This structural analysis suggested that one amino acid, Leu-95, plays a particularly important role in defining the… CONTINUE READING
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