Mutation of the IFNAR-1 receptor binding site of human IFN-alpha2 generates type I IFN competitive antagonists.

@article{Pan2008MutationOT,
  title={Mutation of the IFNAR-1 receptor binding site of human IFN-alpha2 generates type I IFN competitive antagonists.},
  author={Manjing Pan and Eyal Kalie and Brian J Scaglione and Elizabeth S. Raveche and Gideon Schreiber and Jerome A. Langer},
  journal={Biochemistry},
  year={2008},
  volume={47 46},
  pages={12018-27}
}
Type I interferons (IFNs) are multifunctional cytokines that activate cellular responses by binding a common receptor consisting of two subunits, IFNAR-1 and IFNAR-2. Although the binding of IFNs to IFNAR-2 is well characterized, the binding to the lower affinity IFNAR-1 remains less well understood. Previous reports identified a region of human IFN-alpha2 on the B and C helices ("site 1A": N65, L80, Y85, Y89) that plays a key role in binding IFNAR-1 and contributes strongly to differential… CONTINUE READING
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