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PubMed · 11419948

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

F J Moy·E Diblasio·J Wilhelm·R Powers
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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.

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Amino Acid SequenceCrystallography, X-RayDimerizationHumansInterleukin-13Interleukin-13 Receptor alpha1 SubunitInterleukin-4Models, BiologicalModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryReceptors, InterleukinReceptors, Interleukin-13Receptors, Interleukin-4Sequence AlignmentSignal TransductionSolutionsComparative StudyJournal Article

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F J Moy, E Diblasio, J Wilhelm, R Powers. 2001-06-29. Solution structure of human IL-13 and implication for receptor binding.. https://doi.org/10.1006/jmbi.2001.4764

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