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. 2018 Feb 26;9:821. doi: 10.1038/s41467-018-03219-7

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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. 8 — Induced fit binding of ligand to IGF-1R and IR. a Proposed kinetic scheme. S1, S2: site 1 and site 2 on one receptor monomer; S1΄, S2΄: site 1 and site 2 on the opposing receptor monomer. Black filled circle: hot ligand (i.e., IGF-I, IGF-II or insulin). Grey circle: cold ligand (i.e., IGF-I, IGF-II or insulin). a₁ and d₁: ligand association and dissociation rate constants for the high-affinity site. a₂ and d₂: ligand association and dissociation rate constants for doubly liganded, symmetrical receptor conformation. a₃ and d₃: association and dissociation rate constant for binding of a third insulin molecule (IR only, not applicable to IGF-1R). b Plot for accelerated dissociation of a pre-bound tracer-labelled ligand by cold (unlabelled) ligand. The dissociation time was 20 min. The experimental data were as described previously (reproduced in Supplementary Table 4)¹⁸ and are shown as blue triangles for IGF-1 and red diamonds for insulin, with the fit of the induced-fit model to these data shown as lines (IGF-I blue; insulin red)