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Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexes
- Source :
- Protein Science. 8:482-489
- Publication Year :
- 2008
- Publisher :
- Wiley, 2008.
-
Abstract
- 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.
- Subjects :
- 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
Subjects
Details
- ISSN :
- 09618368
- Volume :
- 8
- Database :
- OpenAIRE
- Journal :
- Protein Science
- Accession number :
- edsair.doi.dedup.....bc374fe03a4155056b56d14291545fef