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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, conserved sites in C-terminal regions of FGF19 and FGF21 mediate interaction with β-Klotho. (A) Binding of human FGF proteins to soluble human β-Klotho measured by AlphaScreen. (B,C) Inhibition of β-Klotho binding to (B) FGF21 and (C) FGF19 in the same AlphaScreen. The curves represent mean ± SD of three independent experiments performed in triplicates. EC₅₀ and IC₅₀ values represent mean ± SD of three independent experiments. (D,E) IC₅₀ values against (D) FGF21 and (E) FGF19 determined from the AlphaScreen assay described above for FGF19 C-terminal mutant peptides. IC₅₀ values are expressed as fold change relative to WT peptide. *Curve did not converge.