Structure of IL-22 Bound to Its High-Affinity IL-22R1 Chain

Academic Article

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. © 2008 Elsevier Ltd. All rights reserved.
  • Published In

  • Structure  Journal
  • Digital Object Identifier (doi)

    Author List

  • Jones BC; Logsdon NJ; Walter MR
  • Start Page

  • 1333
  • End Page

  • 1344
  • Volume

  • 16
  • Issue

  • 9