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. 2023 Sep 25;8:364. doi: 10.1038/s41392-023-01625-y

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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. 2 — Key residues for the interaction between MK-6892 and HCAR2. a Structural comparison of the binding modes of niacin, MMF and MK-6892 to HCAR2. b The detailed interactions between MK-6892 and HCAR2 in OBP (left panel) and EBP (right panel). Black dashed lines represent polar interactions. c Mutagenesis effects of the residues in OBP and EBP of HCAR2 on their activities in response to niacin and MK-6892 stimulation examined by cAMP inhibition assay. The value of ΔpEC₅₀ (pEC₅₀MT-pEC₅₀WT) shows differences between wild-type (WT) receptors and mutants (MT). Data are displayed as mean ± SEM from at least three independent experiments, each performed in triplicate. Statistical significance was determined by one-way analysis of variance with Dunnett’s multiple comparison test (compared to WT). n.s., no significance. d Structural comparison of the niacin- and MK-6892 bound binding pocket in HCAR2. The conformational changes between the two structures are indicated as red arrows