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. 2022 Mar 18;12:4695. doi: 10.1038/s41598-022-08467-8

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Sequence and structural comparison of IGF-II and insulin. (A) Sequence alignment of IGF-II and insulin. Domains are indicated above. Each peptide has three alpha helices; B-chain helix 1 (black circles), A-chain helix 2 (orange circles) and A-chain helix 3 (red circles). Residue numbers are indicated below each sequence. Insulin YB16 and IGF-II Q18 residues are in solid filled circles. (B) IGF-II and (C) insulin ribbon structures (PDB: 1IGL and 1MSO respectively) show the three disulphide bonds and helices coloured as in (A). Side chains of YB16 in insulin and Q18 in IGF-II are shown. (D) Schematic diagram representing the IR and IGF-1R ligand bound extracellular domain structures. Individual αβ monomer outlines are coloured either blue or orange. Extracellular domains include the first and second leucine-rich repeat domains (L1 and L2), cysteine-rich domain (CR), first, second and third fibronectin type-III domains (FnIII-1, -2, and -3), insert domain (ID), α-chain C-terminal region (αCT). Transmembrane and intracellular domains, including the tyrosine kinase domain, are not shown. (E) Insulin and (F) IGF-II bound to site 1 of their cognate receptors, as highlighted with the black box in (D) (from PDB: 6HN5 and 6VWI, respectively). L1 domains are surface filled in cornflower blue, α-chain C-terminal regions (αCT) are coloured purple. The side chains of insulin residue YB16 and F39 of the IR L1 domain and the equivalent residues Q18 in IGF-II and S35 of the IGF-1R L1 domain are shown with transparent surface fill.