Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site

Academic Article


  • Interleukin 10 (IL-10) is a dimeric cytokine that plays a central role in suppressing inflammatory responses. These activities are dependent on the interaction of IL-10 with its high-affinity receptor (IL-10R1). This intermediate complex must subsequently recruit the low-affinity IL-10R2 chain before cell signaling can occur. Here we report the 2.9 Å crystal structure of IL-10 bound to a soluble form of IL-10R1 (sIL-10R1). The complex consists of two IL-10s and four sIL-10R1 molecules. Several residues in the IL-10/sIL-10R1 interface are conserved in all IL-10 homologs and their receptors. The data suggests that formation of the active IL-10 signaling complex occurs by a novel molecular recognition paradigm where IL-10R1 and IL-10R2 both recognize the same binding site on IL-10.
  • Published In

  • Immunity  Journal
  • Digital Object Identifier (doi)

    Author List

  • Josephson K; Logsdon NJ; Walter MR
  • Start Page

  • 35
  • End Page

  • 46
  • Volume

  • 15
  • Issue

  • 1