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. 2019 Jul 24;5(7):eaaw7935. doi: 10.1126/sciadv.aaw7935

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Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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Fig. 6 — Lipid-channel interactions. (A) Side and top views of ribbon diagrams of the TRPC5 tetramer: four CHS molecules and four PLs (potentially ceramide-1-phosphate or phosphatidic acid) are shown as spheres with purple or yellow carbons, respectively. (B) Side views of each CHS and PL molecules per protomer. (C and D) Ribbon diagram of the TRPC5 lipid binding regions. (C) PL interacts with the pore helix through Trp⁵⁷⁷ and Phe⁵⁷⁶. (D) CHS, shown in purple, interacts with the S4/S5 linker at Asn⁵⁰⁰ and the N-terminal domains at Trp³¹⁵, Tyr³¹⁶, and Trp³²². (E and F) Patch clamp recordings of lipid binding site mutants in response to EA.