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. 2022 Jul 30;13:4434. doi: 10.1038/s41467-022-32214-2

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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 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. 1 — a Schematic diagram of human ALS, IGFBP3, and IGF1. Each domain is labeled above the diagram, and the amino acids are numbered under the diagram. In IGFBP3, the central linker domain, which was not resolved in the cryo-EM map, is shown as a dashed line. The boundary of the central linker domain is labeled with a red C and N, indicating the C-terminus of NBP3 and N-terminus of CBP3, respectively. b Size-exclusion chromatography (SEC) profile of human IGF1/IGFBP3/ALS ternary complex (left) and SDS-PAGE analysis of the SEC peak fractions stained with Coomassie blue (right). Pooled fractions for cryo-EM analysis are marked with the bar (violet). Similar results were observed in three independent experiments. c Overall structure of the human IGF1/IGFBP3/ALS ternary complex. Cryo-EM maps (top) and the corresponding cartoon models (bottom) of the ternary complex are shown. ALS, N-terminal domain of IGFBP3 (NBP3), C-terminal domain of IGFBP3 (CBP3), and IGF1 are in violet, blue, cyan, and yellow, respectively. The C-terminal end of NBP3 and N-terminal end of CBP3 are marked with red dots. Disulfide bridges (orange) and N-linked glycans (green) are shown as sticks.