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

Immunity. 2001 Jul;15(1):35-46. doi: 10.1016/s1074-7613(01)00169-8.


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 A 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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallization
  • Interferon gamma Receptor
  • Interleukin-10 / chemistry*
  • Molecular Sequence Data
  • Receptors, Interferon / chemistry
  • Receptors, Interleukin / chemistry*
  • Receptors, Interleukin-10


  • Receptors, Interferon
  • Receptors, Interleukin
  • Receptors, Interleukin-10
  • Interleukin-10

Associated data

  • PDB/1J7V