Structure of the extracellular domains of the human interleukin-6 receptor  -chain Academic Article uri icon

abstract

  • Dysregulated production of IL-6 and its receptor (IL-6R) are implicated in the pathogenesis of multiple myeloma, autoimmune diseases and prostate cancer. The IL-6R complex comprises two molecules each of IL-6, IL-6R, and the signaling molecule, gp130. Here, we report the x-ray structure (2.4 A) of the IL-6R ectodomains. The N-terminal strand of the Ig-like domain (D(1)) is disulfide-bonded to domain D(2), and domains D(2) and D(3), the cytokine-binding domain, are structurally similar to known cytokine-binding domains. The head-to-tail packing of two closely associated IL-6R molecules observed in the crystal may be representative of the configuration of the physiological dimer of IL-6R and provides new insight into the architecture of the IL-6R complex.

authors

  • Varghese, JN
  • Moritz, RL
  • Lou, M-Z
  • van Donkelaar, A
  • Ji, H
  • Ivancic, N
  • Branson, KM
  • Hall, NE
  • Simpson, RJ

publication date

  • December 10, 2002