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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. 3 — A ITC measurements of the DARPin A5 interacting with the SAM domain 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 DARPin A5 in complex with the p63 SAM domain shown in two different orientations rotated by 90°. C Pulldown experiments with different in-vitro translated p63 isoforms and immobilized DARPin A5. Only p63 isoforms containing a SAM domain are bound by DARPin A5. 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 A5 with purified full-length TAp63α and ΔNp63α isoforms. Both dimeric (TAp63α) and tetrameric (ΔNp63α) bind to the SAM domain.