Structure of the activating IL-1 receptor signaling complex

Nat Struct Mol Biol. 2012 Mar 18;19(4):455-7. doi: 10.1038/nsmb.2260.


Interleukin-1 (IL-1)-family cytokines are mediators of innate and adaptive immunity. They exert proinflammatory effects by binding a primary receptor that recruits a receptor accessory protein to form a signaling-competent heterotrimeric complex. Here we present the crystal structure of IL-1β bound to its primary receptor IL-1RI and its receptor accessory protein IL-1RAcP, providing insight into how IL-1-type cytokines initiate signaling and revealing an evolutionary relationship with the fibroblast growth factor receptor family.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Humans
  • Interleukin-1 Receptor Accessory Protein / chemistry*
  • Interleukin-1 Receptor Accessory Protein / metabolism
  • Interleukin-1beta / chemistry*
  • Interleukin-1beta / metabolism
  • Models, Molecular
  • Protein Conformation
  • Receptors, Interleukin-1 Type I / chemistry*
  • Receptors, Interleukin-1 Type I / metabolism
  • Signal Transduction


  • Interleukin-1 Receptor Accessory Protein
  • Interleukin-1beta
  • Receptors, Interleukin-1 Type I

Associated data

  • PDB/4DEP