Crystallization and preliminary X-ray diffraction analysis of the interleukin-3 alpha receptor bound to the Fab fragment of antibody CSL362.

@article{Broughton2014CrystallizationAP,
  title={Crystallization and preliminary X-ray diffraction analysis of the interleukin-3 alpha receptor bound to the Fab fragment of antibody CSL362.},
  author={Sophie E Broughton and Timothy R. Hercus and Tracy L. Nero and Urmi Dhagat and Catherine Mary Owczarek and Matthew Philip Hardy and Louis Jerry Fabri and Pierre D. Scotney and Andrew D. Nash and Nicholas J. Wilson and Angel F Lopez and Michael W Parker},
  journal={Acta crystallographica. Section F, Structural biology communications},
  year={2014},
  volume={70 Pt 3},
  pages={358-61}
}
Interleukin-3 (IL-3) is a member of the beta common family of cytokines that regulate multiple functions of myeloid cells. The IL-3 receptor-specific alpha subunit (IL3Rα) is overexpressed on stem cells/progenitor cells of patients with acute myeloid leukaemia, where elevated receptor expression correlates clinically with a reduced patient survival rate. The monoclonal antibody (MAb) CSL362 is a humanized MAb derived from the murine MAb 7G3, originally identified for its ability to specifically… CONTINUE READING