Partial agonist/antagonist mouse interleukin-2 proteins indicate that a third component of the receptor complex functions in signal transduction
| Autor: | J. L. Imler, G. Zurawski, S. M. Zurawski |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Receptor complex
Glutamine Biology Binding Competitive General Biochemistry Genetics and Molecular Biology Structure-Activity Relationship Cell surface receptor Enzyme-linked receptor Animals 5-HT5A receptor Cloning Molecular Binding site Receptor Molecular Biology Aspartic Acid Binding Sites General Immunology and Microbiology General Neuroscience Receptors Interleukin-2 Biological activity Cell biology Kinetics Biochemistry Interleukin-2 Signal transduction Research Article Signal Transduction |
| Zdroj: | The EMBO Journal. 9:3899-3905 |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1990.tb07610.x |
| Popis: | Some mouse interleukin-2 (mIL-2) proteins with substitutions at residue Gln141 are unable to trigger a maximal biological response. The Asp141 protein induces the lowest maximal response. The Asp141 protein can weakly antagonize the biological activity of mIL-2 and strongly antagonizes the biological activity of active mIL-2 mutant proteins that have defects in interactions with the high affinity receptor. Residue 141 mutant proteins bind with reduced affinity to T cells expressing the high affinity IL-2 receptor, yet bind normally to transfected fibroblasts expressing only the alpha and beta chains of the receptor. These results suggest that a third receptor component is important for both binding and signal transduction. |
| Databáze: | OpenAIRE |
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