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pubmed-article:3676333pubmed:abstractTextAlignment of the sequences, the identification of conserved residue patterns and secondary structure predictions indicate that the extra-cellular regions of the human and Drosophila epidermal growth factor (EGF), c-erb-B2 and human insulin receptors each contain two large, homologous domains (L) which are probably comprised of at least four short alpha-helices followed by turns of conserved length and beta-strands. In the human and Drosophila EGF and c-erb-B2 receptors these homologous domains are each followed by a series of smaller cystine-rich domains (S) to give a gene-duplicated structure of 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. There are two 'hyper-variable' regions, one at the end of the large domains and one in the cystine-rich sequences, which are candidates for hormone or growth-factor binding.lld:pubmed
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pubmed-article:3676333pubmed:articleTitleOn the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors.lld:pubmed
pubmed-article:3676333pubmed:affiliationLudwig Institute for Cancer Research, University College, London, U.K.lld:pubmed
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