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. 2018 Jan 26;9:386. doi: 10.1038/s41467-017-02633-7

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Crystal structure of the IL-3 binary complex. a The structure of IL3Rα (coloured blue-grey in all panels) bound to the four α-helical bundle of IL-3 (coloured purple in all panels). The β-strands that make up the three FnIII domains (NTD, D2 and D3) and the N- and C-termini are labelled. The cysteine residues in IL3Rα are represented as yellow spheres and the bound sugars at N80, N109 and N218 of ILRα are shown as sticks. The mutated N212Q residue is shown as red spheres. D197 is represented as green spheres. b A close-up view highlighting key interactions between IL-3 and the IL3Rα NTD (site 1b). Hydrogen bonds are shown as black dashed lines in all panels. c A close-up view highlighting key interactions between IL-3 and the IL3Rα D2–D3 linker region (part of site 1a). d A close-up view highlighting key interactions between IL-3 and the IL3Rα D3 (part of site 1a). Together, c and d define the complete site 1a