Crystal structure of human epidermal growth factor and its dimerization.

@article{Lu2001CrystalSO,
  title={Crystal structure of human epidermal growth factor and its dimerization.},
  author={Hongliang Lu and Jinchun Chai and Mi Li and Bing Ren Huang and Chuan Hua He and Ru Chang Bi},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 37},
  pages={
          34913-7
        }
}
Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be… CONTINUE READING

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Crystal Structure of Human Epidermal Growth Factor

  • P. J. Kraulis
  • J. Appl. Crystallogr
  • 1993
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