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. 2018 Jul 23;8:11045. doi: 10.1038/s41598-018-29396-5

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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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Two distinct sites in C-terminal region of FGF21 interact with β-Klotho. (A) Amino acid sequence alignment of C-terminal regions of human FGF19, FGF21 and FGF23. Residues that are identical between FGF19, FGF21 and FGF23 are colored red. (B) Binding of WT Fc-FGF21 to soluble human β-Klotho measured by solid-phase binding assay. Results are normalized to the response at the highest concentration of Fc-FGF21 protein. The curve represents mean ± SD of three independent experiments performed in duplicates. (C,D) EC₅₀ values determined from the solid-phase binding assay of Fc-FGF21 (C) alanine and (D) arginine mutants. Values are expressed as fold change relative to WT protein. Gaps were inserted to align the two graphs. *Curve did not converge. (E) Binding of FGF21 and WT Fc-FGF21 to human β-Klotho measured by bio-layer interferometry. K_D values were estimated using a 1:1 binding model. (F,G) Linear regression analysis of K_D determined by bio-layer interferometry versus EC₅₀ determined by solid-phase binding assay for Fc-FGF21 (F) alanine and (G) arginine mutants. Values represent mean ± SD of three independent experiments.