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• W2073526502 abstract "Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer. Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects. The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs. Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand anchor points interspersed among ligand-specific interactions that tune the relative IFN-binding affinities, in an apparent extracellular ligand proofreading mechanism that modulates biological activity. Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns." @default.
• W2073526502 created "2016-06-24" @default.
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• W2073526502 date "2011-08-01" @default.
• W2073526502 modified "2023-10-17" @default.
• W2073526502 title "Structural Linkage between Ligand Discrimination and Receptor Activation by Type I Interferons" @default.
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• W2073526502 doi "https://doi.org/10.1016/j.cell.2011.06.048" @default.
• W2073526502 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3166218" @default.
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