Solution structure of human IL-13 and implication for receptor binding

Franklin J. Moy, Elizabeth Diblasio, James Wilhelm, Robert Powers

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

Interleukin-13 has been implicated as a key factor in asthma, allergy, atopy and inflammatory response, establishing the protein as a valuable therapeutic target. The high-resolution solution structure of human IL-13 has been determined by multidimensional NMR. The resulting structure is consistent with previous short-chain left-handed four-helix bundles, where a significant similarity in the folding topology between IL-13 and IL-4 was observed. IL-13 shares a significant overlap in biological function with IL-4, a result of the common α chain component (IL-4Rα) in their respective receptors. Based on the available structural and mutational data, an IL-13/IL-4Rα model and a sequential mechanism for forming the signaling heterodimer is proposed for IL-13.

Original languageEnglish (US)
Pages (from-to)219-230
Number of pages12
JournalJournal of Molecular Biology
Volume310
Issue number1
DOIs
StatePublished - Jun 29 2001

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Keywords

  • Interleukin-13
  • Interleukin-4
  • NMR
  • Solution structure

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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