An unusual cytokine:Ig-domain interaction revealed in the crystal structure of leukemia inhibitory factor (LIF) in complex with the LIF receptor

By T. Huyton, Jian‐guo Zhang, C. Luo, M. Lou, D. Hilton, N. Nicola, Thomas P. J. Garrett. 2007

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Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex (2008, methodology): “search model individual domains of mouse LIF-R from the LIF-R/LIF structure (PDB ID 2Q7N) (Huyton et al., 2007).”
The molecular details of cytokine signaling via the JAK/STAT pathway (2018, background): “These cytokine/receptor complexes are not built around two gp130 chains but instead are built around a heterodimer between gp130 and another JAK-binding tall receptor called LIFRβ.57,58 As is the case for IL-6, these cytokines first bind to cytokine-specific nonsignaling alpha receptor chains and th”
The composition and signaling of the IL-35 receptor are unconventional (2012, background): “Finally, a previously unknown mode of binding may exist that uses the site 1-2-3 model in a manner not predicted on the basis of the existing structural information for IL-6, LIF and CNT”
Structural insights into the assembly and activation of the IL‐27 signaling complex (2022, unknown): “Elevated levels of IL-27 gene signatures are found in cancer and are associated with poor prognoses (Jia et al , 2016).”