The structure of human interleukin-11 reveals receptor-binding site features and structural differences from interleukin-6

Acta Crystallogr D Biol Crystallogr. 2014 Sep;70(Pt 9):2277-85. doi: 10.1107/S1399004714012267. Epub 2014 Aug 23.


Interleukin (IL)-11 is a multifunctional member of the IL-6 family of cytokines. Recombinant human IL-11 is administered as a standard clinical treatment for chemotherapy-induced thrombocytopaenia. Recently, a new role for IL-11 signalling as a potent driver of gastrointestinal cancers has been identified, and it has been demonstrated to be a novel therapeutic target for these diseases. Here, the crystal structure of human IL-11 is reported and the structural resolution of residues previously identified as important for IL-11 activity is presented. While IL-11 is thought to signal via a complex analogous to that of IL-6, comparisons show important differences between the two cytokines and it is suggested that IL-11 engages GP130 differently to IL-6. In addition to providing a structural platform for further study of IL-11, these data offer insight into the binding interactions of IL-11 with each of its receptors and the structural mechanisms underlying agonist and antagonist variants of the protein.

Keywords: GP130; JAK; STAT3; cytokine; interleukin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Humans
  • Interleukin-11 / chemistry*
  • Interleukin-11 / metabolism
  • Interleukin-6 / chemistry*
  • Models, Molecular
  • Protein Conformation
  • Receptors, Interleukin-11 / metabolism*
  • Ultracentrifugation


  • Interleukin-11
  • Interleukin-6
  • Receptors, Interleukin-11

Associated data

  • PDB/4MHL