| Literature DB >> 11419948 |
F J Moy1, E Diblasio, J Wilhelm, R Powers.
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 alpha chain component (IL-4Ralpha) in their respective receptors. Based on the available structural and mutational data, an IL-13/IL-4Ralpha model and a sequential mechanism for forming the signaling heterodimer is proposed for IL-13. Copyright 2001 Academic Press.Entities:
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Year: 2001 PMID: 11419948 DOI: 10.1006/jmbi.2001.4764
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469