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Crystallization and preliminary X‐ray diffraction of human interleukin‐7 bound to unglycosylated and glycosylated forms of its α‐receptor

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The interleukin‐7 (IL‐7) signaling pathway plays an essential role in the development, proliferation and homeostasis of T and B cells in cell‐mediated immunity. Understimulation and overstimulation of the IL‐7 signaling pathway leads to severe combined immunodeficiency, autoimmune reactions, heart disease and cancers. Stimulation of the IL‐7 pathway begins with IL‐7 binding to its α‐receptor, IL‐7Rα. Protein crystals of unglycosylated and glycosylated complexes of human IL‐7–IL‐7Rα extracellular domain (ECD) obtained using a surface entropy‐reduction approach diffract to 2.7 and 3.0 Å, respectively. Anomalous dispersion methods will be used to solve the unglycosylated IL‐7–IL‐7Rα ECD complex structure and this unglycosylated structure will then serve as a model in molecular‐replacement attempts to solve the structure of the glycosylated IL‐7–α‐receptor complex.
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Keywords: interleukin‐7

Document Type: Research Article

Affiliations: Department of Molecular and Cellular Biochemistry, Comprehensive Cancer Center, Ohio State University, 467 Hamilton Hall, 1645 Neil Avenue, Columbus, OH 43210, USA

Publication date: October 1, 2007

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