A structural template for gp130-cytokine signaling assemblies

Dar Chone Chow, Lena Brevnova, Xiao Lin He, Monika M. Martick, Alex Bankovich, K. Christopher Garcia*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

26 Scopus citations


The gp130-cytokine system has been fertile ground for protein structure-function studies aimed at elucidating the basis of ligand recognition and receptor activation. A number of longstanding questions involve the mechanism of the stepwise assembly of the active signaling complexes, as well as the structure of the gp130-cytokine complexes. It has been clear from functional studies that the paradigm of gp130-cyokine recognition will differ substantially from the classical homo-dimeric systems, typified by human growth hormone (hGH) and its receptor. Recently, a crystal structure of a viral interleukin-6 (vIL-6), complexed with the D1D2D3 domains of the gp130 extracellular domain, has resolved many of these questions, and reconciled much of the functional and mutagenesis data which have existed for a variety of gp130-cytokines. In this review, we discuss the structure of the vIL-6/gp130 complex in some detail and suggest that the geometry of this complex will be a common structural template utilized by other gp130-cytokines, as well as cytokines from distinct signaling systems.

Original languageEnglish (US)
Pages (from-to)225-235
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number3
StatePublished - Nov 11 2002


  • Complex
  • Cytokine
  • Receptor
  • Recognition
  • Signaling
  • Structure
  • X-ray crystallography

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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