ArticleProtein science : a publication of the Protein Society1999
Solution assembly of the pseudo-high affinity and intermediate affinity interleukin-2 receptor complexes.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Engineered cytokine/antibody fusion proteins improve IL-2 delivery to pro-inflammatory cells and promote antitumor activity.JCI insight · 2024Article
- Engineering IL-2 for immunotherapy of autoimmunity and cancer.Nature reviews. Immunology · 2022Review
- Structural biology of shared cytokine receptors.Annual review of immunology · 2009Review
- The structure of IL2 bound to the three chains of the IL2 receptor and how signaling occurs.Medical immunology (London, England) · 2006Article
- Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
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Authors and funding
6 authors.
Funding
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.
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Registered trials
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