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Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):358-61. doi: 10.1107/S2053230X14002593. Epub 2014 Feb 19.

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

Author information

1
Australian Cancer Research Foundation Rational Drug Discovery Centre and Biota Structural Biology Laboratory, St Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
2
Division of Human Immunology, The Centre for Cancer Biology, SA Pathology, Adelaide, South Australia, Australia.
3
CSL Limited, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australia.

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.

KEYWORDS:

IL-3 receptor-specific alpha subunit; cytokines; interleukin-3

PMID:
24598927
PMCID:
PMC3944702
DOI:
10.1107/S2053230X14002593
[Indexed for MEDLINE]
Free PMC Article
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