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. 2015 Sep 30;6:8297. doi: 10.1038/ncomms9297

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(a) Location of key residues identified by mutagenesis (with the side chain shown in red) mapped to the cryo-EM structure (closed state). Turret and pore helix are shown in orange and green, respectively. (b) Molecular docking of RhTx (coloured by surface electrostatic potential: red, negatively charged; blue, positively charged) to TRPV1, using the DkTx-bound state as the starting template. The backbone of TRPV1 and DkTx are shown in grey and red, respectively, with the electron density map superimposed. (c) Comparison of channel conformations between the closed state (grey) and RhTx-bound open state (orange).