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. 2023 May 22;6:549. doi: 10.1038/s42003-023-04935-7

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© The Author(s) 2023

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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Fig. 3 — a Cartoon representation of the atomic model of sulindac-bound hMRP4 (left). Cryogenic electron microscopy map of sulindac-bound hMRP4 (right). b Electron microscopy density of sulindac in the same orientation as (A) (left). Sulindac is inserted into a pocket formed by the hydrophobic residues of hMRP4 (right). Contour level is 0.424. c Coordination of sulindac by hMRP4. Residues related to substrate binding are shown as sticks. Transmembrane helices (TMs) 2, 5, 6, and 12, which interact with sulindac, are labeled. d Relative ATPase activities of hMRP4 and mutants in a detergent of n-dodecyl-β-D-maltoside and cholesteryl hemisuccinate with 2 mM ATP in the absence of substrate (PGE1) or inhibitor (sulindac). Each data point is the mean of three independent experiments (n = 3), and the error bars represent the mean ± standard deviation. Source data are provided in Supplementary Data 3.