Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein

@article{Mattoon2001IdentificationOT,
  title={Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein},
  author={Dawn R Mattoon and Kushol Gupta and Jeffrey B Doyon and Patrick J. Loll and Daniel DiMaio},
  journal={Oncogene},
  year={2001},
  volume={20},
  pages={3824-3834}
}
We have developed a genetic method to determine the active orientation of dimeric transmembrane protein helices. The bovine papillomavirus E5 protein, a 44-amino acid homodimeric protein that appears to traverse membranes as a left-handed coiled-coil, transforms fibroblasts by binding and activating the platelet-derived growth factor (PDGF) β receptor. A heterologous dimerization domain was used to force E5 monomers to adopt all seven possible symmetric coiled-coil registries relative to one… CONTINUE READING

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