Structural domains of the insulin receptor and IGF receptor required for dimerisation and ligand binding
| Autor: | K. Siddle, Cristina Marino-Buslje, L Molina, D.R Quinn |
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| Rok vydání: | 2000 |
| Předmět: |
DNA
Complementary medicine.medical_treatment Molecular Sequence Data Biophysics Peptide CHO Cells Biology Ligands Binding Competitive Biochemistry Insulin-like growth factor Structural Biology Cricetinae Genetics medicine Animals Insulin Amino Acid Sequence Receptor Molecular Biology Ligand binding chemistry.chemical_classification Binding Sites Structural domain Chinese hamster ovary cell Receptors Somatomedin Cell Biology Ligand (biochemistry) Peptide Fragments Receptor Insulin Amino acid Fibronectin Insulin receptor chemistry biology.protein Dimerization |
| Zdroj: | FEBS Letters. 467:226-230 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(00)01161-3 |
| Popis: | We investigated structural requirements for dimerisation and ligand binding of insulin/IGF receptors. Soluble receptor fragments consisting of N-terminal domains (L1/CYS/L2, L1/CYS/L2/F0) or fibronectin domains (F0/F1/F2, F1/F2) were expressed in CHO cells. Fragments containing F0 or F1 domains were secreted as disulphide-linked dimers, and those consisting of L1/CYS/L2 domains as monomers. None of these proteins bound ligand. However, when a peptide of 16 amino acids from the α-subunit C-terminus was fused to the C-terminus of L1/CYS/L2, the monomeric insulin and IGF receptor constructs bound their respective ligands with affinity only 10-fold lower than native receptors. |
| Databáze: | OpenAIRE |
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