Structure and ligand specificity of the Drosophila melanogaster insulin receptor.
作者： R Fernandez-Almonacid , O M Rosen
DOI: 10.1128/MCB.7.8.2718
关键词:
摘要: The insulin-binding and protein tyrosine kinase subunits of the Drosophila melanogaster insulin receptor homolog have been identified characterized by using antipeptide antibodies elicited to deduced amino acid sequence alpha beta human receptor. In D. embryos cell lines, contains 110 or 120 kilodaltons (kDa), a 95-kDa subunit that is phosphorylated on in response intact cells vitro, 170-kDa may be an incompletely processed All components are synthesized from proreceptor, joined disulfide bonds, exposed surface. recognized antibody acids 1142 1162 702 723 proreceptor. Of polypeptide ligands tested, only reacts with Insulinlike growth factors type I II, epidermal factor, silkworm insulinlike prothoracicotropic hormone unable stimulate autophosphorylation. Thus despite evolutionary divergence vertebrates invertebrates, essential features structure intrinsic functions remarkably conserved.
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