ArticleThe Journal of biological chemistry2026
Cryo-EM structure of the interleukin-31 receptor complex defines non-canonical interactions that confer receptor specificity.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Interleukin-31 (IL-31) is a Th2-associated cytokine that induces inflammatory and pruritic diseases through a heterodimeric receptor composed of IL-31Rα and OSMRβ. Although IL-31 has emerged as an important therapeutic target, the molecular mechanism by which IL-31 engages IL-31Rα and OSMRβ to assemble its receptor complex remains poorly defined. Here we report a 3.3 Å cryo-EM structure of the human IL-31/IL-31Rα/OSMRβ complex. The structure reveals that IL-31 assembles its receptors through a site 2-site 3 architecture reminiscent of LIF and OSM, yet employs distinct receptor-recognition features at both interfaces. Site 2 is dominated by a hydrophilic IL-31-IL-31Rα interface that lacks the aromatic anchoring mode observed in LIF and OSM receptor complexes, whereas site 3 adopts a remodeled anchoring mode involving IL-31 K134, T130, and the conserved OSMRβ W267 anchor. Structure-guided mutagenesis and SPR binding analyses support the contributions of site 2 and site 3 interface residues to receptor recognition. Together, these findings reveal how non-canonical interactions at sites 2 and 3 confer receptor specificity within the IL-31 receptor complex.
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