Crystal structure of the IL-15/IL-15Ra complex

File:2z3q.gif


2z3q, resolution 1.85Å

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OverviewOverview

Interleukin 15 (IL-15) and IL-2, which promote the survival of memory, CD8(+) T cells and regulatory T cells, respectively, bind receptor, complexes that share beta- and gamma-signaling subunits. Receptor, specificity is provided by unique, nonsignaling alpha-subunits. Whereas, IL-2 receptor-alpha (IL-2Ralpha) is expressed together in cis with the, beta- and gamma-subunits on T cells and B cells, IL-15Ralpha is expressed, in trans on antigen-presenting cells. Here we present a 1.85-A crystal, structure of the human IL-15-IL-15Ralpha complex. The structure provides, insight into the molecular basis of the specificity of cytokine, recognition and emphasizes the importance of water in generating this very, high-affinity complex. Despite very low IL-15-IL-2 sequence homology and, distinct receptor architecture, the topologies of the IL-15-IL-15Ralpha, and IL-2-IL-2Ralpha complexes are very similar. Our data raise the, possibility that IL-2, like IL-15, might be capable of being presented in, trans in the context of its unique receptor alpha-chain.

About this StructureAbout this Structure

2Z3Q is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor unit presented in trans., Chirifu M, Hayashi C, Nakamura T, Toma S, Shuto T, Kai H, Yamagata Y, Davis SJ, Ikemizu S, Nat Immunol. 2007 Sep;8(9):1001-7. Epub 2007 Jul 22. PMID:17643103

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