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

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

doi:10.1006/jmbi.2001.4764

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

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

Research output: Contribution to journal › Article › peer-review

55 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 language	English (US)
Pages (from-to)	219-230
Number of pages	12
Journal	Journal of Molecular Biology
Volume	310
Issue number	1
DOIs	https://doi.org/10.1006/jmbi.2001.4764
State	Published - Jun 29 2001
Externally published	Yes

Keywords

Interleukin-13
Interleukin-4
NMR
Solution structure

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1006/jmbi.2001.4764

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AU - Wilhelm, James

AU - Powers, Robert

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

Abstract

Keywords

ASJC Scopus subject areas

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