1p9m

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spinqualitylabelsall models 1p9m, resolution 3.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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