Structure of the insulin receptor ectodomain reveals a folded-over conformation

@article{McKern2006StructureOT,
  title={Structure of the insulin receptor ectodomain reveals a folded-over conformation},
  author={Neil M. McKern and Michael C Lawrence and Victor A Streltsov and M Lou and Timothy E. Adams and George O. Lovrecz and Thomas C. Elleman and Kim M. Richards and John D. Bentley and Patricia A. Pilling and Peter A. Hoyne and Kellie A. Cartledge and Tam M. Pham and Jennifer L. Lewis and Sonia E. Sankovich and Violet Stoichevska and Elizabeth N. da Silva and Christine P. Robinson and Maurice J. Frenkel and Lindsay G. Sparrow and Ross T. Fernley and Vidana Chandana Epa and Colin W. Ward},
  journal={Nature},
  year={2006},
  volume={443},
  pages={218-221}
}
The insulin receptor is a phylogenetically ancient tyrosine kinase receptor found in organisms as primitive as cnidarians and insects. In higher organisms it is essential for glucose homeostasis, whereas the closely related insulin-like growth factor receptor (IGF-1R) is involved in normal growth and development. The insulin receptor is expressed in two isoforms, IR-A and IR-B; the former also functions as a high-affinity receptor for IGF-II and is implicated, along with IGF-1R, in malignant… CONTINUE READING
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