The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction.

@article{Meyts1994TheIG,
  title={The insulin-like growth factor-I receptor. Structure, ligand-binding mechanism and signal transduction.},
  author={Pierre De Meyts and Bret Wallach and Claus T Christoffersen and Birgitte Urs\o and K Gr\onskov and Lori J Latus and Fumiatsu Yakushiji and Mapoko M. Ilondo and Ronald M. Shymko},
  journal={Hormone research},
  year={1994},
  volume={42 4-5},
  pages={152-69}
}
The nonclassical binding kinetics of IGF-I and insulin to their respective receptors, suggestive of negative cooperativity, can be readily explained by our recently proposed novel binding mechanism whereby the bivalent ligand bridges the two receptor alpha-subunits alternatively at opposite sites in a symmetrical receptor structure. The bivalent binding mechanism also explains bell-shaped bioactivity curves. The possible role of different binding modes versus differences in downstream signaling… CONTINUE READING

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