Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexes
| Autor: | Michael J. Nemeth, Zining Wu, Thomas M. Laue, Thomas L. Ciardelli, Byron Goldstein, Stefano F. Liparoto |
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| Rok vydání: | 2008 |
| Předmět: |
Receptor complex
Protein Conformation Molecular Sequence Data B-cell receptor Receptors Interleukin-2 Interleukin-17 receptor Biology Interleukin-13 receptor Binding Competitive Biochemistry Recombinant Proteins Interleukin 10 receptor alpha subunit Solutions Radioligand Assay Biopolymers Biophysics Amino Acid Sequence GABBR1 Receptor Ultracentrifugation Molecular Biology Protease-activated receptor 2 Research Article |
| Zdroj: | Protein Science. 8:482-489 |
| ISSN: | 0961-8368 |
| DOI: | 10.1110/ps.8.3.482 |
| Popis: | The high affinity interleukin-2 receptor is composed of three cell surface subunits, IL-2Ralpha, IL-2Rbeta, and IL-2Rgamma. Functional forms of the IL-2 receptor exist, however, that enlist only two of the three subunits. On activated T-cells, the alpha- and beta-subunits combine as a preformed heterodimer (the pseudo-high affinity receptor) that serves to capture IL-2. On a subpopulation of natural killer cells, the beta- and gamma-subunits interact in a ligand-dependent manner to form the intermediate affinity receptor site. Previously, we have demonstrated the feasibility of employing coiled-coil molecular recognition for the solution assembly of a heteromeric IL-2 receptor complex. In that study, although the receptor was functional, the coiled-coil complex was a trimer rather than the desired heterodimer. We have now redesigned the hydrophobic heptad sequences of the coiled-coils to generate soluble forms of both the pseudo-high affinity and the intermediate affinity heterodimeric IL-2 receptors. The properties of these complexes were examined and their relevance to the physiological IL-2 receptor mechanism is discussed. |
| Databáze: | OpenAIRE |
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