Crystal Structure of a Truncated Epidermal Growth Factor Receptor Extracellular Domain Bound to Transforming Growth Factor α

@article{Garrett2002CrystalSO,
  title={Crystal Structure of a Truncated Epidermal Growth Factor Receptor Extracellular Domain Bound to Transforming Growth Factor α},
  author={Thomas P. J. Garrett and Neil M. McKern and Meizhen Lou and Thomas C. Elleman and Timothy E. Adams and George O. Lovrecz and Hong-Jian Zhu and Francesca Walker and Morry J. Frenkel and Peter A. Hoyne and Robert N. Jorissen and Edouard C Nice and Antony W. Burgess and Colin W. Ward},
  journal={Cell},
  year={2002},
  volume={110},
  pages={763-773}
}
We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha. TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues. The results indicate how EGFR family members can bind a family of highly variable ligands. In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule. There are two types of dimers in the asymmetric unit: a… CONTINUE READING
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Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains

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