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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal, Humanized / chemistry*
  • Crystallization
  • Humans
  • Interleukin-3 Receptor alpha Subunit / chemistry*
  • Molecular Sequence Data
  • Protein Binding
  • X-Ray Diffraction

Substances

  • Antibodies, Monoclonal, Humanized
  • IL3RA protein, human
  • Interleukin-3 Receptor alpha Subunit