Journal article

Interleukin-3 binding to the murine beta(IL-3) and human beta c receptors involves functional epitopes formed by domains 1 and 4 of different protein chains

JM Murphy, SC Ford, JE Olsen, SE Gustin, PD Jeffrey, DL Ollis, IG Young

JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2004

Abstract

Interleukin-3 (IL-3) is a cytokine produced by activated T-cells and mast cells that is active on a broad range of hematopoietic cells and in the nervous system and appears to be important in several chronic inflammatory diseases. In this study, alanine substitutions were used to investigate the role of residues of the human beta-common (hbetac) receptor and the murine IL-3-specific (beta(IL-3)) receptor in IL-3 binding. We show that the domain 1 residues, Tyr(15) and Phe(79), of the hbetac receptor are important for high affinity IL-3 binding and receptor activation as shown previously for the related cytokines, interleukin-5 and granulocyte-macrophage colony-stimulating factor, which also ..

View full abstract

University of Melbourne Researchers