1i1r
From Proteopedia
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| , resolution 2.4Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A CYTOKINE/RECEPTOR COMPLEX
Overview
The activation of gp130, a shared signal-transducing receptor for a family of cytokines, is initiated by recognition of ligand followed by oligomerization into a higher order signaling complex. Kaposi's sarcoma-associated herpesvirus encodes a functional homolog of human interleukin-6 (IL-6) that activates human gp130. In the 2.4 angstrom crystal structure of the extracellular signaling assembly between viral IL-6 and human gp130, two complexes are cross-linked into a tetramer through direct interactions between the immunoglobulin domain of gp130 and site III of viral IL-6, which is necessary for receptor activation. Unlike human IL-6 (which uses many hydrophilic residues), the viral cytokine largely uses hydrophobic amino acids to contact gp130, which enhances the complementarity of the viral IL-6-gp130 binding interfaces. The cross-reactivity of gp130 is apparently due to a chemical plasticity evident in the amphipathic gp130 cytokine-binding sites.
About this Structure
1I1R is a Protein complex structure of sequences from Homo sapiens and Human herpesvirus 8. Full crystallographic information is available from OCA.
Reference
Structure of an extracellular gp130 cytokine receptor signaling complex., Chow D, He X, Snow AL, Rose-John S, Garcia KC, Science. 2001 Mar 16;291(5511):2150-5. PMID:11251120
Page seeded by OCA on Sun Mar 30 21:13:22 2008
