Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 10 (October 2007)

crystallization communications

Acta Cryst. (2007). F63, 865-869 [ doi:10.1107/S1744309107042807 ]

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

J. Wickham Jr and S. T. R. Walsh

Abstract: 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 Å, 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.

Keywords: interleukin-7.