Title: Crystallization and preliminary X-ray diffraction analysis of the interleukin-3 alpha receptor bound to the Fab fragment of antibody CSL362
Authors: Broughton, SE
Hercus, TR
Nero, TL
Dhagat, U
Owczarek, CM
Hardy, MP
Fabri, LJ
Scotney, PD
Nash, AD
Wilson, NJ
Lopez, AF
Parker, MW
Issue Year: 2014
Publisher WILEY-BLACKWELL
Series ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS: 70(): 358-361
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 (IL3R alpha) 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 IL3R alpha in complex with the MAb CSL362 has been determined.
URI: https://publications.svi.edu.au/publications/1772
Other Identifiers 10.1107/S2053230X14002593
Publication type Article
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