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
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/