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. 2024 May 2;31(9):1377–1385. doi: 10.1038/s41594-024-01299-2

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© The Author(s) 2024

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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Fig. 5 — a, The closed configuration of TRPV1 with all four subunits occupied by PI lipid. Particle numbers (ptcls) are shown. b, The open configuration of TRPV1 with LPA bound to all four subunits. The VBPs of the A monomers are shown to demonstrate the domain-swap architecture that comprises the VBP (S3, S4 and S4–S5 from A; S5 and S6 from D). c,d, Schematic of the binding pocket from a top-down view highlighting the domain-swap architecture and helical movements between the closed (c) and open (d) conformations. e, Structural changes associated with the binding of LPA compared to apo (transparent black). f–i, Substochiometric states of LPA binding with monomers bound with 1 LPA (f), 2 LPA in opposite pockets (g), 2 LPA in neighboring pockets (h) and 3 LPA (i). The leftmost panels show a cartoon representation of the TRPV1 tetramer indicating the functional state of each VBP monomer. Monomers are labeled anticlockwise; LPA-occupied monomers are shadowed with magenta. The functional state of the pore is indicated as ‘closed’ (π helix at Y671), ‘open’ (α helix at Y671 with S6 moved away from the pore to the same extent as fully occupied LPA) and ‘intermediate’ (‘inter.’, α helix at Y671 with S6 positioned between that of apo and fully occupied LPA).