The carboxyl-terminal domain of insulin-like growth factor-I receptor interacts with the insulin receptor and activates its protein tyrosine kinase
| Autor: | Amanda C. Hayward, Shu-Lian Li, Anatolii P. Koval, Yehiel Zick, John Termini, Yoko Fujita-Yamaguchi, K. Siddle, Derek LeRoith |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular animal structures Carboxyl-terminal domain medicine.medical_treatment Biophysics Stimulation Transfection Polymerase Chain Reaction Biochemistry Homology (biology) Cell Line Receptor IGF Type 1 BIAcore Structural Biology Genetics medicine Animals Protein tyrosine kinase Domain interaction Cloning Molecular Surface plasmon resonance Receptor Molecular Biology Sequence Tagged Sites Binding Sites biology Chemistry Growth factor Insulin Cell Membrane Receptor Protein-Tyrosine Kinases Cell Biology Insulin-like growth factor-I receptor Peptide Fragments Receptor Insulin Recombinant Proteins Rats Cell biology Enzyme Activation Kinetics Insulin receptor biology.protein Tyrosine kinase |
| Zdroj: | FEBS Letters. 421:45-49 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(97)01523-8 |
| Popis: | Receptors for insulin and insulin-like growth factor-I (IR and IGFIR) consisting of the alpha2beta2 structure are protein tyrosine kinases (PTKs). Carboxyl-terminal (CT) domains of their beta subunits are structurally diverse while the PTK domains share the highest homology. Interactions between CT and PTK domains of IR and IGFIR were studied by means of PTK activity, fluorescence energy transfer or surface plasmon resonance using BIAcore. We present evidence that IGFIR CT directly interacts with both IGFIR and IR. Although binding to both receptors, stimulation of PTK activity only occurs with IR but not IGFIR. |
| Databáze: | OpenAIRE |
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