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. 2018 Sep 21;9:3860. doi: 10.1038/s41467-018-06192-3

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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. 2 — Structural organisation of representative insulin-like proteins. a human insulin (hINS in the sequence box)(PDB ID: 1mso), b human IGF-1 (1gzr), c human IGF-2 (hormone ligand taken from 3kr3 complex), d D. melanogaster DILP5 (2wfv). A-chains or domains (in IGF1/IGF2) are in coral, B-chains/domains in white, C-and D-domains in IGF-1/IGF-2 in green and blue, respectively (untraced residues in IGF-1 in green dashed line). The white insulin B-chain in a shows its T-conformation, while the red part of the B-helix depicts the R-conformer of the B1-B8 part of insulin B-chain