1i1r
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(New page: 200px<br /> <applet load="1i1r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1r, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:18, 12 November 2007
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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 4. 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 Mon Nov 12 17:25:20 2007
