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. 2023 Jun 17;14:3613. doi: 10.1038/s41467-023-39307-6

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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. 4 — a CBD binds to the fenestration enclosed by repeats IV and I of Na_v1.7. The surrounding environment, which is highly hydrophobic, is shown as the hydrophobic surface, calculated in ChimeraX. b The local structures around the F-site (left) remain nearly identical in apo (PDB: 7W9K) and CBD-bound Na_v1.7. Surrounding residues are shown as sticks. The only potential hydrogen bond is shown as red dashed lines. c F-site mutations weaken the inhibition of Na_v1.7 by CBD. Both single point mutations V383A and F387A reduced the sensitivity of Na_v1.7 to CBD, with the IC₅₀ right-shifted from 1.82 ± 0.10 μM to 3.56 ± 0.58 μM and 3.65 ± 0.78 μM, respectively. Nav1.7-WT, n = 1, 5, 12, 8, 7. Nav1.7-F387A, n = 4, 6, 4. Nav1.7–V383A, n = 5, 4,5. Data are presented as mean ± SEM. n biological independent cells. d CBD shares similar binding poses in Na_v1.7 and TRPV2 at the F-site. A similar fenestration binding site for CBD in Na_v1.7 and in TRPV2 is seen in the superimposed structures. A side view (left) and a top view (right) of the comparison between CBD-bound Na_v1.7 (domain colored) and TRPV2 (pink, PDB: 6U88) are shown.