Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/101854
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Type: Journal article
Title: Crystallization and preliminary X-ray diffraction analysis of the interleukin-3 alpha receptor bound to the Fab fragment of antibody CSL362
Author: Broughton, S.
Hercus, T.
Nero, T.
Dhagat, U.
Owczarek, C.
Hardy, M.
Fabri, L.
Scotney, P.
Nash, A.
Wilson, N.
Lopez, A.
Parker, M.
Citation: Acta Crystallographica Section F: Structural Biology Communications, 2014; 70(3):358-361
Publisher: International Union of Crystallography
Issue Date: 2014
ISSN: 2053-230X
2053-230X
Statement of
Responsibility: 
Sophie E. Broughton, Timothy R. Hercus, Tracy L. Nero, Urmi Dhagat, Catherine M. Owczarek, Matthew P. Hardy, Louis J. Fabri, Pierre D. Scotney, Andrew D. Nash, Nicholas J. Wilson, Angel F. Lopez and Michael W. Parkerar
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: Crystallization
Rights: © 2014 International Union of Crystallography All rights reserved
RMID: 0030050955
DOI: 10.1107/S2053230X14002593
Appears in Collections:Medicine publications

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