Structural basis for the lower affinity of the insulin-like growth factors for the insulin receptor.

@article{Gauguin2008StructuralBF,
  title={Structural basis for the lower affinity of the insulin-like growth factors for the insulin receptor.},
  author={Lisbeth Gauguin and Birgit Klaproth and Waseem Sajid and Asser Sloth Andersen and Kerrie A. McNeil and Briony E Forbes and Pierre De Meyts},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 5},
  pages={2604-13}
}
Insulin and the insulin-like growth factors (IGFs) bind with high affinity to their cognate receptor and with lower affinity to the noncognate receptor. The major structural difference between insulin and the IGFs is that the IGFs are single chain polypeptides containing A-, B-, C-, and D-domains, whereas the insulin molecule contains separate A- and B-chains. The C-domain of IGF-I is critical for high affinity binding to the insulin-like growth factor I receptor, and lack of a C-domain largely… CONTINUE READING

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