Structure of an Extracellular gp130 Cytokine Receptor Signaling Complex

By D. Chow, Xiao-lin He, A. Snow, S. Rose‐John, K. Garcia. 2001

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IL-6 signal transduction and its physiological roles: the signal orchestration model. (2003, background): “2001); (3) two trimolecular complexes are assembled together via IL-6 site 3 and the Ig-like domain of gp130 (Moritz et al. 1999; Chow et al. 2001), as well as through site 4, completing the hexameric complex, which is competent to generate intracellular signals (Somers et al.”
Interleukin-6 Family Cytokines. (2018, background): “The direct binding of vIL-6 to gp130 without the assistance of the IL-6R was shown by the crystal structure of the complex of gp130 and vIL-6 (Chow et al. 2001).”
Non-Canonical Interleukin 23 Receptor Complex Assembly (2014, background): “The loop connecting the C-D helices of p19 represents the site III interface with IL-23R because it contains the characteristic hot spot site III tryptophan 157 (human, Trp-156; murine, Trp-157) conserved among all gp130 cytokines, including Trp-157 in human IL-6 or Trp-144 in viral IL-6 (27).”
Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex (2008, background): “Up to this point, only the architecture of the cytokine binding region of symmetric homodimeric complexes of gp130 with IL-6 or IL-11 have been elucidated (Boulanger et al., 2003b; Chow et al., 2001; Matadeen et al., 2007).”
Convergent mechanisms for recognition of divergent cytokines by the shared signaling receptor gp130. (2003, unknown): “the ␣ carbons) (Chow et al., 2001)”