1P9M

Crystal structure of the hexameric human IL-6/IL-6 alpha receptor/gp130 complex

Summary for 1P9M

• Entry DOI: 10.2210/pdb1p9m/pdb
• Descriptor: Interleukin-6 receptor beta chain, Interleukin-6, Interleukin-6 receptor alpha chain (3 entities in total)
• Functional Keywords: ig domain, four helix bundle, cytokine, interleukin-6, gp130, signaling protein-cytokine complex, signaling protein/cytokine
• Biological source: Homo sapiens (human); More
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P40189; Secreted: P05231; Isoform 1: Basolateral cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P08887
• Total number of polymer chains: 3
• Total formula weight: 78253.48

Authors

Boulanger, M.J.,Chow, D.C.,Brevnova, E.E.,Garcia, K.C. (deposition date: 2003-05-12, release date: 2003-07-01, Last modification date: 2024-11-13)

Primary citation

Boulanger, M.J.,Chow, D.C.,Brevnova, E.E.,Garcia, K.C.
Hexameric Structure and Assembly of the Interleukin-6/IL-6 alpha-Receptor/gp130 Complex
Science, 300:2101-2104, 2003

PubMed Abstract: Interleukin-6 (IL-6) is an immunoregulatory cytokine that activates a cell-surface signaling assembly composed of IL-6, the IL-6 alpha-receptor (IL-6Ralpha), and the shared signaling receptor gp130. The 3.65 angstrom-resolution structure of the extracellular signaling complex reveals a hexameric, interlocking assembly mediated by a total of 10 symmetry-related, thermodynamically coupled interfaces. Assembly of the hexameric complex occurs sequentially: IL-6 is first engaged by IL-6Ralpha and then presented to gp130in the proper geometry to facilitate a cooperative transition into the high-affinity, signaling-competent hexamer. The quaternary structures of other IL-6/IL-12 family signaling complexes are likely constructed by means of a similar topological blueprint.

PubMed: 12829785
DOI: 10.1126/science.1083901

Experimental method

X-RAY DIFFRACTION (3.65 Å)