Structure-Function Studies of Growth-Factor Receptors

  • Mona Bajaj
  • Michael D. Waterfield
  • Thomas L. Blundell
Part of the NATO ASI Series book series (NSSA, volume 133)


The extracellular regions of the human and drosphila EGF, c-erb-2 and human insulin receptors each contain two large, homologous domains (L) which are probably comprised of at least four α-helices followed by turns of conserved lengths and β-strands. In the human and drosphila EGF and c-erb-2 receptors these homologous domains are each followed by a series of smaller cystine rich domains (S) to give a gene duplicafied structure L1S11S12S13L2S21S22S23. In the human insulin receptor the second series of cystine domains is replaced by a different sequence. These duplicated structures are probably organised as a pseudo-symmetrical dimer contained within one chain with a “hypervariable” region at one end. This region is a candidate for hormone or growth-factor binding.


Epidermal Growth Factor Receptor Epidermal Growth Factor Human Epidermal Growth Factor Receptor Insulin Receptor Duplicate Sequence 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Mona Bajaj
    • 1
  • Michael D. Waterfield
    • 1
  • Thomas L. Blundell
    • 1
    • 2
  1. 1.Research Fund, Lincoln’s Inn FieldsLudwig Institute for Cancer Research at the Imperial CancerLondonUK
  2. 2.Dept. of CrystallographyBirkbeck CollegeLondonUK

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