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Signaling conformations of the tall cytokine receptor gp130 when in complex with IL-6 and IL-6 receptor.
- Source :
-
Nature Structural & Molecular Biology . Jun2005, Vol. 12 Issue 6, p545-551. 7p. - Publication Year :
- 2005
-
Abstract
- gp130 is a shared cytokine signaling receptor and the founding member of the 'tall' class of cytokine receptors. A crystal structure of the ligand-binding domains of gp130 in complex with human interleukin-6 (IL-6) and its a-receptor (IL-6Rα) revealed a hexameric architecture in which the gp130 membrane-distal regions were∼100Å apart, in contrast to the close apposition seen between short cytokine receptor complexes. Here we used single-particle EM to visualize the entire extracellular hexameric IL-6–IL-6Rα–gp130 complex, containing all six gp130 domains. The structure reveals that gp130 is bent such that the membrane-proximal domains of gp130 are close together at the cell surface, enabling activation of intracellular signaling. Variation in the receptor bend angles suggests a possible conformational transition from open to closed states upon ligand binding; this transition is probably representative of the other tall cytokine receptors. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 15459993
- Volume :
- 12
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Nature Structural & Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 17230962
- Full Text :
- https://doi.org/10.1038/nsmb941