Structure and mechanism of receptor sharing by the IL-10R2 common chain

Academic Article


  • IL-10R2 is a shared cell surface receptor required for the activation of five class 2 cytokines (IL-10, IL-22, IL-26, IL-28, and IL-29) that play critical roles in host defense. To define the molecular mechanisms that regulate its promiscuous binding, we have determined the crystal structure of the IL-10R2 ectodomain at 2.14 Å resolution. IL-10R2 residues required for binding were identified by alanine scanning and used to derive computational models of IL-10/IL-10R1/IL-10R2 and IL-22/IL-22R1/IL-10R2 ternary complexes. The models reveal a conserved binding epitope that is surrounded by two clefts that accommodate the structural and chemical diversity of the cytokines. These results provide a structural framework for interpreting IL-10R2 single nucleotide polymorphisms associated with human disease. © 2010 Elsevier Ltd.
  • Published In

  • Folding & design  Journal
  • Digital Object Identifier (doi)

    Author List

  • Yoon SI; Jones BC; Logsdon NJ; Harris BD; Deshpande A; Radaeva S; Halloran BA; Gao B; Walter MR
  • Start Page

  • 638
  • End Page

  • 648
  • Volume

  • 18
  • Issue

  • 5