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. 2022 Jul 18;12:12241. doi: 10.1038/s41598-022-16193-4

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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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HOIP NZF1 binds NEMO and ubiquitin simultaneously. (A) Crystal packing of the heteropentameric structure indicates interaction of a proximal ubiquitin from a symmetry-related molecule with HOIP NZF1. (B) Sequence alignment and superimposition of HOIP NZF1 and Npl4 NZF. The conserved residues involved in interactions with ubiquitin are highlighted in red. (C) HOIP NZF1 uses distinct surfaces for binding NEMO and ubiquitin. Amino acid residues from HOIP NZF1 interacting with NEMO or ubiquitin are highlighted green and magenta, respectively. (D,E) Surface plasmon resonance (SPR) analysis of HOIP NZF1 interaction with ubiquitin and NEMO, indicating equilibrium dissociation constant (K_D) values of 135.2 ± 8.4 µM and 86.7 ± 7.1 µM (K_D ± SE), respectively.