ArticleeLife2022
Structure of the IL-27 quaternary receptor signaling complex.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- Same-Slide Spatial Multiomics Integration with IN-DEPTH Reveals Tumor Virus-Linked Spatial Reorganization of the Tumor Microenvironment.Cancer discovery · 2026Article
- Cytokine multimerization: when more is more and sometimes less.Nature reviews. Immunology · 2026Review
- IL-27: A Double-Edged Sword in Immune Regulation via JAK-STAT Orchestration.Journal of immunology research · 2026Review
- Free Epstein-Barr virus-induced gene 3 functions as an autonomous immunosuppressive cytokine to maintain immune tolerance.Frontiers in immunology · 2026Article
- IL-27 promotes Treg cell expression of CD122 and fitness at homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Interleukin-27-adipose-derived mesenchymal stromal cell-based gene therapy attenuates inflammation in lipopolysaccharide-induced acute respiratory distress syndrome.Stem cell research & therapy · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Article
- IL-27 attenuated macrophage injury and inflammation induced by Mycobacterium tuberculosis by activating autophagy.In vitro cellular & developmental biology. Animal · 2025Article
- Structures of complete extracellular assemblies of type I and type II Oncostatin M receptor complexes.Nature communications · 2024Article
- Structure of the interleukin-5 receptor complex exemplifies the organizing principle of common beta cytokine signaling.Molecular cell · 2024Article
- Structural insights into IL-11-mediated signalling and human IL6ST variant-associated immunodeficiency.Nature communications · 2024Article
- IL-27 expression regulation and its effects on adaptive immunity against viruses.Frontiers in immunology · 2024Review
- The Human GP130 Cytokine Receptor and Its Expression-an Atlas and Functional Taxonomy of Genetic Variants.Journal of clinical immunology · 2023Review
- Molecular cloning, characterization and gene expression analysis of twelve interleukins in obscure pufferFish and shellfish immunology reports · 2023Article
- Evolutionarily conserved IL-27β enhances Th1 cells potential by triggering the JAK1/STAT1/T-bet axis in Nile tilapia.Fish and shellfish immunology reports · 2023Article
- Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant.Nature communications · 2023Article
- Human interleukin-12α and EBI3 are cytokines with anti-inflammatory functions.Science advances · 2023Article
- Structural insights into the assembly of gp130 family cytokine signaling complexes.Science advances · 2023Article
- Structural basis of activation and antagonism of receptor signaling mediated by interleukin-27.Cell reports · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Interleukin 27 (IL-27) is a heterodimeric cytokine that functions to constrain T cell-mediated inflammation and plays an important role in immune homeostasis. Binding of IL-27 to cell surface receptors, IL-27Rα and gp130, results in activation of receptor-associated Janus Kinases and nuclear translocation of Signal Transducer and Activator of Transcription 1 (STAT1) and STAT3 transcription factors. Despite the emerging therapeutic importance of this cytokine axis in cancer and autoimmunity, a molecular blueprint of the IL-27 receptor signaling complex, and its relation to other gp130/IL-12 family cytokines, is currently unclear. We used cryogenic-electron microscopy to determine the quaternary structure of IL-27, composed of p28 and Epstein-Barr Virus-Induced 3 (Ebi3) subunits, bound to receptors, IL-27Rα and gp130. The resulting 3.47 Å resolution structure revealed a three-site assembly mechanism nucleated by the central p28 subunit of the cytokine. The overall topology and molecular details of this binding are reminiscent of IL-6 but distinct from related heterodimeric cytokines IL-12 and IL-23. These results indicate distinct receptor assembly mechanisms used by heterodimeric cytokines with important consequences for targeted agonism and antagonism of IL-27 signaling.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.