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. 2024 Jan 15;20(2):75–97. doi: 10.1038/s44320-023-00005-6

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© The Author(s) 2024

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/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) Schematic of the domain architecture of PNKP and TRIM37 with indication of top predicted interfaces. Numbers in blue indicate the motif interface pLDDT for the respective interface. Roman numbering refers to structural models in (B) and (C). (B) Structural model of interface i shown in (A) with labeled residues that were mutated. (C) Structural model of interface ii shown in (A). (D) BRET titration curves are shown for wildtype interaction and mutants for two biological replicates, each with three technical replicates. Protein acceptor over protein donor expression levels are plotted on the x-axis determined from fluorescence and luminescence measurements, respectively. The BRET trajectory could not be fitted because of an unusual saturation behavior (see methods for details). (E) Schematic of the domain architecture of ESRRG and PSMC5 with indication of top predicted interfaces. Numbers in blue indicate the motif interface pLDDT for the respective interface. Roman numbering refers to structural models in (F) and (G). (F) Structural model of interface iii shown in (E) with labeled residues that were mutated. (G) Structural model of interface iv shown in (E). (H) BRET titration curves are shown for wildtype interaction and mutants of ESRRG-PSMC5 pairs for two biological replicates, each with three technical replicates. Protein acceptor over protein donor expression levels are plotted on the x-axis determined from fluorescence and luminescence measurements, respectively. In panels (B), (C), (F), and (G) motif sequences are indicated at the bottom. Gray letters indicate residues not predicted to bind. Source data are available online for this figure.