Title:	Crystallisation and preliminary X-ray diffraction analysis of the Interleukin-3 alpha receptor bound to Fab fragment of antibody
Authors:	Dhagat, U Lopez, AF Nero, TL Wilson, NJ Hercus, TR Nash, AD Broughton, SE Scotney, PD Fabri, LJ Hardy, MP Owczarek, CM Parker, MW
Issue Year:	2014
Publisher
Series	Acta Crystallogr F Struct Biol Commun.:
Abstract	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 recognize the human IL-3 receptor and for blocking the signalling of IL-3 in myeloid and endothelial cells. In order to elucidate the molecular mechanism of CSL362 antagonism, a preliminary structure of human IL3Rα in complex with the MAb CSL362 has been determined.
URI:	https://publications.svi.edu.au/publications/2421
Other Identifiers	70(Pt 3):358-61
Publication type	Article
Grant ID	GNT0559001; GNT0565217; GNT1021645;
Find it online	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944702/