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Crystallization and preliminary X-ray diffraction of human interleukin-7 bound to unglycosylated and glycosylated forms of its alpha-receptor.

Wickham J, Walsh ST

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

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 alpha-receptor, IL-7R alpha. Protein crystals of unglycosylated and glycosylated complexes of human IL-7-IL-7R alpha extracellular domain (ECD) obtained using a surface entropy-reduction approach diffract to 2.7 and 3.0 A, respectively. Anomalous dispersion methods will be used to solve the unglycosylated IL-7-IL-7R alpha 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-alpha-receptor complex.

Published 2 October 2007 in Acta Crystallogr Sect F Struct Biol Cryst Commun, 63: 865-9.
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