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 Citations (Scopus)

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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Interleukin-13 Receptors
Interleukin-13
Interleukin-4
Hypersensitivity
Asthma
human interleukin-13
Proteins

Keywords

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

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Solution structure of human IL-13 and implication for receptor binding. / Moy, Franklin J.; Diblasio, Elizabeth; Wilhelm, James; Powers, Robert.

In: Journal of Molecular Biology, Vol. 310, No. 1, 29.06.2001, p. 219-230.

Research output: Contribution to journalArticle

Moy, Franklin J. ; Diblasio, Elizabeth ; Wilhelm, James ; Powers, Robert. / Solution structure of human IL-13 and implication for receptor binding. In: Journal of Molecular Biology. 2001 ; Vol. 310, No. 1. pp. 219-230.
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