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    Structure. 2008 Sep 10;16(9):1333-44. doi: 10.1016/j.str.2008.06.005. Epub 2008 Jul 3.

    Structure of IL-22 bound to its high-affinity IL-22R1 chain.

    Jones BC, Logsdon NJ, Walter MR.

    Source

    Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

    Abstract

    IL-22 is an IL-10 family cytokine that initiates innate immune responses against bacterial pathogens and contributes to immune disease. IL-22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-10R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL-22R1 also pairs with the IL-20R2 chain to induce IL-20 and IL-24 signaling. To define the molecular basis of these diverse interactions, we have determined the structure of the IL-22/sIL-22R1 complex. The structure, combined with homology modeling and surface plasmon resonance studies, defines the molecular basis for the distinct affinities and specificities of IL-22 and IL-10 receptor chains that regulate cellular targeting and signal transduction to elicit effective immune responses.

    PMID:
    18599299
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2637415
    Free PMC Article

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