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. 2023 Nov 20;17(1):2281714. doi: 10.1080/19336950.2023.2281714

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© 2023 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The terms on which this article has been published allow the posting of the Accepted Manuscript in a repository by the author(s) or with their consent.

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Figure 11. — Receptor site for the deathstalker scorpion toxin LqhIII on Na_V1.5. a) spacefilling side view and top view of Na_V1.5 (gray) with LqhIII bound (purple). b) close-up view of bound LqhIII (purple) to its receptor site on the Na_V1.5 backbone structure. Inset. higher resolution image of the interface between LqhIII and Na_V1.5. c) superposition of the voltage sensor in the unmodified activated state and the toxin-modified partially activated state. d) mutational map of the interface residues in the LqhIII receptor site illustrated with “open book” format. LqhIII, purple; Na_V1.5, blue. Amino acid residues highlighted in yellow and orange are required for high-affinity binding. Adapted from Jiang et al., 2021 [168].