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TitleStructural insights into the assembly and activation of the IL-27 signaling complex.
Journal, issue, pagesEMBO Rep, Vol. 23, Issue 10, Page e55450, Year 2022
Publish dateOct 6, 2022
AuthorsYibo Jin / Paul K Fyfe / Scott Gardner / Stephan Wilmes / Doryen Bubeck / Ignacio Moraga /
PubMed AbstractInterleukin 27 (IL-27) is a heterodimeric cytokine that elicits potent immunosuppressive responses. Comprised of EBI3 and p28 subunits, IL-27 binds GP130 and IL-27Rα receptor chains to activate the ...Interleukin 27 (IL-27) is a heterodimeric cytokine that elicits potent immunosuppressive responses. Comprised of EBI3 and p28 subunits, IL-27 binds GP130 and IL-27Rα receptor chains to activate the JAK/STAT signaling cascade. However, how these receptors recognize IL-27 and form a complex capable of phosphorylating JAK proteins remains unclear. Here, we used cryo electron microscopy (cryoEM) and AlphaFold modeling to solve the structure of the IL-27 receptor recognition complex. Our data show how IL-27 serves as a bridge connecting IL-27Rα (domains 1-2) with GP130 (domains 1-3) to initiate signaling. While both receptors contact the p28 component of the heterodimeric cytokine, EBI3 stabilizes the complex by binding a positively charged surface of IL-27Rα and Domain 1 of GP130. We find that assembly of the IL-27 receptor recognition complex is distinct from both IL-12 and IL-6 cytokine families and provides a mechanistic blueprint for tuning IL-27 pleiotropic actions.
External linksEMBO Rep / PubMed:35920255 / PubMed Central
MethodsEM (single particle)
Resolution4.0 Å
Structure data

14427

7z0l

EMDB-14427, PDB-7z0l:
IL-27 signalling complex
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
KeywordsCYTOKINE / immunosuppression / EBI3 / IL-27R-alpha / gp130 / p28.

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