Figure 1 | Scientific Reports

Figure 1

From: Atomistic mechanisms of human TRPA1 activation by electrophile irritants through molecular dynamics simulation and mutual information analysis

Figure 1

The structure of TRPA1 as determined by cryo EM. (A) Cartoon representation of the pore-closed structure 6PQQ, prepared for simulation (see “Methods”, Structure Preparation). Two monomer units are visible, coloured red and “chocolate” and the approximate position of the membrane is indicated by the grey rectangle. Residues V961 (green), C621 (orange) and C665 (cyan) are indicated as vdW spheres. Segments on chain A that are used in the mutual information analysis are coloured blue (V961-V1005, loop above pocket lid (H7), TRP-like (TRPL) domain and transmembrane domain (TMD) helix (part of S6)), green (Y706-L730, voltage-sensor like domain (VSLD) helix threaded through loop above pocket lid (S1)), and purple (Y842-V865 (VSLD helix (S4)) and connected TMD helix immediately adjoining V961 (S5)). ARD is short for ankyrin repeat domain, IFH is the interfacial helix, and CC indicates coiled-coil. (B) TRPA1 rotated through 90° looking down the channel pore and showing the constriction at the V961 residues, (C) Topology cartoon of TRPA1 (adapted from Suo et al.40).

Back to article page