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. 2018 Jun 12;8:8957. doi: 10.1038/s41598-018-27089-7

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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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NCAM2 FnIII domains bind to FGFR1. Surface plasmon resonance analysis was utilized to investigate interactions between the NCAM2 FnIII1, FnIII2, and FnIII1-2 domains and the ectodomain of FGFR1. Approximately 1000 resonance units (RUs) of the FGFR1β ectodomain (Ig2-Ig3) were immobilized on a sensor chip and recombinant NCAM2 FnIII1 (a), FnIII2 (b) and FnIII1-2 (c) were injected at the indicated concentrations. Binding is expressed as the response difference between the binding of the respective recombinant proteins to a cell on the sensor chip with the immobilized FGFR1β and a control cell on the same sensor chip coated with IgG (d). On the basis of the presented steady state affinity fit curves, K_d values of 0.29 (χ² = 0.057), 4.4 (χ² = 0.016) and 0.13 (χ² = 0.028) μM were estimated for NCAM2 FnIII1 (d), FnIII2 (e) and FnIII1-2 (f), respectively.