Identification of a direct interaction between interleukin 2 and the p64 interleukin 2 receptor gamma chain
| Autor: | R J Robb, Thomas P. Leary, Paul M. Sondel, Stephan D. Voss |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1993 |
| Předmět: |
Interleukin 2
Lymphoma Macromolecular Substances Protein subunit Interleukin 5 receptor alpha subunit Molecular Sequence Data Biology Interleukin 10 receptor alpha subunit Epitopes Interleukin 26 medicine Tumor Cells Cultured Humans Electrophoresis Gel Two-Dimensional Amino Acid Sequence Receptor Interleukin 12 receptor beta 1 subunit Common gamma chain Multidisciplinary Antibodies Monoclonal Receptors Interleukin-2 Thymus Neoplasms Recombinant Proteins Models Structural Spectrometry Fluorescence Biochemistry Biophysics Interleukin-2 Electrophoresis Polyacrylamide Gel medicine.drug Research Article |
| Popis: | The interleukin 2 receptor (IL-2R) consists of at least two subunits, alpha and beta, both of which can bind interleukin 2 (IL-2). Recent studies have demonstrated the existence of a third subunit, a 64-kDa molecule termed IL-2R gamma chain, and have suggested that gamma chain functions to regulate the rate of IL-2 dissociation from the receptor. In the present report we have addressed whether the gamma chain modulates IL-2R affinity by contributing contact sites for IL-2 binding. Using reagents that allow the IL-2R complex to be immunoprecipitated through the IL-2 molecule itself, we demonstrate the existence of a stable IL-2-IL-2R gamma-chain complex. These studies thus establish that the IL-2R gamma chain directly contributes to the IL-2-binding site, consistent with the hypothesis that gamma chain influences IL-2R affinity through its direct interaction with IL-2. |
| Databáze: | OpenAIRE |
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