Literature DB >> 24598927

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

Sophie E Broughton1, Timothy R Hercus2, Tracy L Nero1, Urmi Dhagat1, Catherine M Owczarek3, Matthew P Hardy3, Louis J Fabri3, Pierre D Scotney3, Andrew D Nash3, Nicholas J Wilson3, Angel F Lopez2, Michael W Parker1.   

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.

Entities:  

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

Mesh:

Substances:

Year:  2014        PMID: 24598927      PMCID: PMC3944702          DOI: 10.1107/S2053230X14002593

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


  22 in total

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