title: On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors.
abstract: Alignment 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.
authors: Ludwig Institute for Cancer Research, University College, London, U.K.
authors: M
authors: M
authors: Bajaj
authors: M D
authors: MD
authors: Waterfield
authors: J
authors: J
authors: Schlessinger
authors: W R
authors: WR
authors: Taylor
authors: T
authors: T
authors: Blundell
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003553:Cystine / Q000032:analysis; D004330:Drosophila; D066246:ErbB Receptors / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D005810:Multigene Family; D011487:Protein Conformation; D011972:Receptor, Insulin / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship
chemical_list: D046911:Macromolecular Substances; D003553:Cystine; D066246:ErbB Receptors; D011972:Receptor, Insulin