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. 2022 Jun 18;29(12):2445–2458. doi: 10.1038/s41418-022-01030-y

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — A ITC measurements of the DARPin 8F1 interacting with the TD of p63. The top diagram displays the raw measurement and the bottom diagram shows the integrated heat per titration step. The K_D value is given for the interaction. B Crystal structure of the DARPin 8F1 in complex with the p63 TD showing a 2:1 stoichiometry in two different orientations that are rotated by 90^°. C Pulldown experiments with different in-vitro translated p63 isoforms and immobilized DARPin 8F1. The results show that only open and tetrameric isoforms that exhibit a complete TD bind to the DARPin. The pulldown efficiency relative to the whole protein expression is displayed on the y-axis (n = 3). D Fluorescence anisotropy measurements of Alexa 488 labeled DARPin 8F1 with purified full-length TAp63α and ΔNp63α isoforms. Only the tetrameric ΔNp63α isoform binds strongly while only a negligible interaction is detected for dimeric TAp63α.