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. 2018 Oct 10;9:4192. doi: 10.1038/s41467-018-06493-7

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© The Author(s) 2018

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 — The putative mechanism of PtdIns(3,5)P₂ and ML-SA1 cooperation. a PtdIns(3,5)P₂ induces the π-cation interaction of Y355 and R403 in PtdIns(3,5)P₂/ML-SA1 bound structure. b The molecular detail of Y355 and R403 in the ML-SA1 bound structure (PDB: 5WJ9). c Structural comparison of both agonists bound (cyan) and the ML-SA1 bound (gray) hTRMPL1 structures. d The comparison of the pore region of both agonists bound and the ML-SA1 bound (gray) hTRMPL1 structures