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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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Heme binding to IL-36α and its effects on the protein supported by molecular docking and MD simulation studies. (A–C) The structure of wild-type IL-36α (grey) with two heme molecules (orange) docked at C136 (green) and Y108 (red), respectively (H109, blue). Wireframe surfaces drawn around both binding sites (C136, Y108) represent surfaces of IL-36α residues that make contact with the heme molecule as predicted by the docking algorithm (A). A zoom in at Y108 (B, Y108, red; H109, blue) and C136 (C, C136, green; P137, blue). Residues that stabilize the heme-bound conformation (yellow) are labeled. (D) Comparative per-residue root mean squared fluctuation (RMSF) profiles of the heme bound (red) and the free states (black) of the protein. The RMSF profiles were generated from 200 ns equilibration MD simulations of the free protein and the protein-heme complex. Clear reduction of fluctuations from their mean position is noticed for several amino acids in the heme-bound state indicating the effect of heme binding to the protein.