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. 2023 Oct 2;55(10):2147–2161. doi: 10.1038/s12276-023-01101-1

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© The Author(s) 2023

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. 7 — a The cryo-EM structure of extended T-shaped IR bound to two S597 (PDB ID: 8DTL). b The cryo-EM structure of partial domains of IR bound to IM459 (PDB ID: 7U6D). Detailed binding mode of S597 (c) and IM459 (d). Both peptides bind to site-1 and site-2’ simultaneously, similar to the A62 in the arrowhead-shaped IR, which forms a bridge. e Proposed model of the functional selectivity of IR. Cross-linking between L1 and FnIII-1’ with the dissociation of αCT′ from L1 establishes the intermediate state of IR, which may be critical for its metabolic effects.