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Updated: Jul 31, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

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Structure of the extracellular domains of the human interleukin-6 receptor alpha -chain

J N Varghese1, R L Moritz, M-Z Lou

  • 1Biomolecular Research Institute and Commonwealth Scientific and Industrial Research Organization Health Sciences and Nutrition, 343 Royal Parade, Parkville 3052, Australia.

Proceedings of the National Academy of Sciences of the United States of America
|December 4, 2002
PubMed

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.

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