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. 2020 Jul 8;10:11207. doi: 10.1038/s41598-020-67466-9

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© The Author(s) 2020

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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Structure of DimDAF-12 ligand binding domain model. The model of DimDAF-12_LBD (A and B) was constructed using Modeller and the coordinates of the crystal from Ancylostoma ceylanicum DAF-12 (pdb:3up0) and Strongyloides stercoralis DAF-12 (3gyt). Similar to the other members of the nuclear receptor family, DimDAF-12 exhibits 13 helices and three β-strands, which are packed in a three-layer α-helical sandwich to create a ligand binding pocket, where the DAs were found to bind in the case of AceDAF-12 and SstDAF-12. α-helices were either shown in teal or marine to distinguish them, β-strands were colored in yellow and the loops in teal. All images were generated using PyMol 1.3 (https://pymol.org/2/).