Following the Assembly of Receptor Complex

doi:10.1126/stke.2003.189.tw254

Account Information

Guest Alerts | Access Rights | My Account | Sign In

Site Navigation

Article Views

Abstract
Print View

Article Tools

Help & Feedback

My Science Signaling

Sci. STKE, 1 July 2003
Vol. 2003, Issue 189, p. tw254
[DOI: 10.1126/stke.2003.189.tw254]

EDITORS' CHOICE

STRUCTURAL BIOLOGY Following the Assembly of Receptor Complex

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 ${alpha}$ -receptor (IL-6R ${alpha}$ ), and the extracellular activation and binding domains of gp130. The hexamer assembles sequentially; a binary complex between IL-6R ${alpha}$ 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 ${alpha}$ -receptor/gp130 complex. Science 300, 2101-2104 (2003). [Abstract] [Full Text]

Citation: Following the Assembly of Receptor Complex. Sci. STKE 2003, tw254 (2003).