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. 2019 Nov 15;9:16893. doi: 10.1038/s41598-019-53231-0

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© The Author(s) 2019

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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Structural analysis of IL-36α. (A) NMR structure of IL-36α with numbered β-sheet elements indicated by cyan arrows, α-helical elements in red/yellow and loop regions in grey. (B) Stereoview of the 20 best energy minimized conformers. Flexible loops are indicated and the flexible N-terminal residues, the C136P137, and Y108H109 sites are colored (Met1-Thr9 – red, Cys136Pro137 – gold, Tyr108His109 – magenta). (C–E) Bundle of the IL-36α-heme complex (IL-36α backbone in blue, heme in orange) (C). Detailed view of the heme coordination at Cys136 (D) and Tyr108 (E).