Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.

@article{Sato2000CharacterizationOT,
  title={Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.},
  author={Christine Sato and Jong Ho Kim and Yoshito Abe and Kyuichi Saito and Shigeyuki Yokoyama and Daisuke Kohda},
  journal={Journal of biochemistry},
  year={2000},
  volume={127 1},
  pages={65-72}
}
The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation. We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ). The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type… CONTINUE READING