IL-5 binding to IL-5R on target cells induces rapid tyrosine phosphorylation and activation of various cellular proteins, including JAK1/JAK2 and STAT1/STAT5. Here, we report the crystal structure of dimeric IL-5 in complex with the IL-5RA extracellular domains.

Dec 7, 2011 · To investigate the mechanism underlying ligand-receptor recognition, we determined the structure of IL-5 bound to the extracellular domain of IL-5Rα. IL-5 makes contact with all three fibronectin III-like domains of IL-5Rα, with …

May 16, 2024 · We present the cryo-EM structure of the human IL-5 ternary receptor complex, revealing architectural principles for IL-5, GM-CSF, and IL-3. In mammalian cell culture, single-molecule imaging confirms hexameric IL-5 complex formation on cell surfaces.

Mar 30, 2012 · Here, we report the crystal structure of dimeric IL-5 in complex with the IL-5RA extracellular domains. The structure revealed that IL-5RA sandwiches the IL-5 homodimer by three tandem domains, arranged in a “wrench-like” architecture.

A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF. Cell. 1991 Sep 20;66(6):1175–1184. doi: 10.1016/0092-8674(91)90040-6.

Dec 28, 2011 · IL-5 binding to IL-5R on target cells induces rapid tyrosine phosphorylation and activation of various cellular proteins, including JAK1/JAK2 and STAT1/STAT5. Here, we report the crystal structure of dimeric IL-5 in complex with the IL-5RA extracellular domains.

Interleukin 5 (IL-5) is an interleukin produced by type-2 T helper cells and mast cells. Through binding to the interleukin-5 receptor, interleukin 5 stimulates B cell growth and increases immunoglobulin secretion—primarily IgA. It is also a key mediator in eosinophil activation.

May 13, 1993 · INTERLEUKIN-5 (IL-5) is a lineage-specific cytokine for eosinophilpoiesis and plays an important part in diseases associ-ated with increased eosinophils, such as asthma 1,2. Human IL-5 is a...

Human IL5 migrates by SDS-PAGE as a single band at 32 kDa under non-reducing conditions and 16 kDa under reducing conditions (dithiothreitol, see Fig. 1 A), confirming that the Drosophila hIL5 is a disulfide-linked dimer. Human IL5 was eluted from Superose 12 …

Jan 26, 2001 · A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF