This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1p9m
From Proteopedia
|
Crystal structure of the hexameric human IL-6/IL-6 alpha receptor/gp130 complex
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[147620], Osteopenia/osteoporosis OMIM:[147620]
About this Structure
1P9M is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex., Boulanger MJ, Chow DC, Brevnova EE, Garcia KC, Science. 2003 Jun 27;300(5628):2101-4. PMID:12829785
Page seeded by OCA on Mon Nov 12 18:41:30 2007
