Abstract
Natural killer (NK) cells are lymphocytes of the innate immune system specialized in recognition and killing of certain virus-infected and tumor cells. To carry out this task, NK cells are equipped with a complex array of germ line encoded receptors. These receptors deliver either positive or negative signals, and a delicate balance between these signals governs the NK cell cytolytic activity against the target cell. IRp60 (CD300a) is a human NK inhibitory receptor with an immunoglobulin-like fold. In the present study the IRp60 protein was expressed in Escherichia coli as inclusion bodies and refolded by dilution. The refolded protein was purified to homogeneity, biochemical characterized and the solution structure was investigated using small-angle X-ray scattering (SAXS). The SAXS data revealed that IRp60 is monomeric in solution with a molecular shape characteristic of the immunoglobulin-like structures. A homology model of IRp60 was built and validated experimentally against the SAXS data.
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