Structure-Function Studies of Growth-Factor Receptors
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.
KeywordsEpidermal Growth Factor Receptor Epidermal Growth Factor Human Epidermal Growth Factor Receptor Insulin Receptor Duplicate Sequence
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- Schejter, E.D., Glazer, L., Segal., D., Ullrich, A., Schlessinger, J., and Shilo, B.-Z., 1986, submitted for publication.Google Scholar