The IL-4 Receptor — Signaling Mechanisms

  • Achsah Keegan
  • Keats Nelms
  • William E. Paul
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 365)

Abstract

Interleukin-4 (IL-4) is a multifunctional cytokine that is a member of the hematopoietin family1. Its structure consists of a bundle of four left handed α helices in which the first and second and the third and fourth helices are connected by long over hand loops2,3,4,5. IL-4 is produced by CD4+ T cells1 and by basophils and mast cells6 in response to receptor-mediated stimulation. It mediates its functions by binding to high affinity receptors expressed on a wide range of hematopoeitic and non-hematopoietic cell types7. The molecule defined as the IL-4 receptor (IL-4R) possesses an extracellular domain that is a member of the hematopoeitin-receptor family8. Its cytosolic domain is ~500 amino acids in length and lacks both endogenous tyrosine kinase and nucleotide-binding motifs9. The IL-4R does possess two acid rich regions and sequences homologous to the Box 1 region defined for the gp130 component of the IL-6 receptor10.

Keywords

Tyrosine Phosphorylation Cytosolic Domain Fourth Helix Receptor Gamma Chain Acid Rich Region 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Achsah Keegan
    • 1
  • Keats Nelms
    • 1
  • William E. Paul
    • 1
  1. 1.Laboratory of ImmunologyNational Institute of Allergy and Infectious DiseasesBethesdaUSA

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