Editors' ChoiceStructural Biology

Following the Assembly of Receptor Complex

Science's STKE  01 Jul 2003:
Vol. 2003, Issue 189, pp. tw254-TW254
DOI: 10.1126/stke.2003.189.tw254

Gp130 is a shared signal-transducing receptor for a family of four-helix bundle cytokines including the proinflammatory cytokine interleukin-6 (IL-6). Signaling through the gp130 receptor is critical to the normal growth and differentiation of numerous tissue types. Boulanger et al. have determined the 3.65 angstrom resolution structure of a multicomponent receptor complex comprising human IL-6, the extracellular binding domains of human IL-6 α-receptor (IL-6Rα), and the extracellular activation and binding domains of gp130. The hexamer assembles sequentially; a binary complex between IL-6Rα and IL-6 binds to gp130, and this step facilitates a cooperative transition to the signaling-competent hexamer.

M. J. Boulanger, D.-c. Chow, E. E. Brevnova, K. C. Garcia, Hexameric structure and assembly of the interleukin-6/IL-6 α-receptor/gp130 complex. Science 300, 2101-2104 (2003). [Abstract] [Full Text]