Fig. 4: The C-terminal coiled-coil domain of dTRPA1-A isoform undergoes a large movement during state transitions. | Cell Discovery

Fig. 4: The C-terminal coiled-coil domain of dTRPA1-A isoform undergoes a large movement during state transitions.

From: Molecular architecture and gating mechanisms of the Drosophila TRPA1 channel

Fig. 4: The C-terminal coiled-coil domain of dTRPA1-A isoform undergoes a large movement during state transitions.The alternative text for this image may have been generated using AI.

a Interactions between the C-terminal coiled-coil domain and surrounding ARD in state-2 structure of dTRPA1-A isoform. The C-terminal coiled-coil domain and ARD of state-2 are coloured cyan and marine, respectively. b Compared with the state-2 structure, the coiled-coil domain has a large downward movement with ~12–13 Å in the state-1 structure. The C-terminal coiled-coil domain and ARD of state-1 are coloured orange and grey, respectively. c Interactions between the C-terminal coiled-coil domain and surrounding ARD in state-1 structure of dTRPA1-A isoform. Two views are shown here. d Heat-induced current densities for WT dTRPA1-A and the C-terminal mutants. Independent experiments were repeated for at least four times for each construct (n = 6 for all, except D1156A/E1157A where n = 4). ns not significant, *P = 0.0267, and **P = 0.0088 for WT versus mutants (one-way ANOVA with Dunnett’s multiple comparisons test). Data are mean ± s.e.m. e NMM-induced current densities at −60 mV for WT dTRPA1-A and the C-terminal mutants. Independent experiments were repeated six times for each construct (n = 6 for all). ns not significant, *P = 0.042, **P = 0.0013 and ****P < 0.0001 for WT versus mutants (one-way ANOVA with Dunnett’s multiple comparisons test). Data are mean ± s.e.m. For d and e, the same values for the WT channel are used as in Fig. 3d, e for consistent comparison since all the electrophysiological data were acquired using the same batch of cells.

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