Figure 6 | Scientific Reports

Figure 6

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

Figure 6

(A) Overlaid structures for pocket open pore-open (6V9X, green,) and pocket-closed pore-closed (6PQQ, red). The section of a single monomer unit between the pore (at V961) and the binding pocket lid (at K671, only present for pocket-open structure 6V9X) is shown. Strong pairwise mutual information exchanges are shown with green arrows for 6V9X and red arrows for 6PQQ. Side chains are shown only for 6V9X, except for Y726, N845, and V961 where 6PQQ side chains are shown for comparison. The protein segment is shown viewed across the plane of the monomer unit. (B) and (C) comparison of pocket- and pore-closed with pocket and pore-open structures highlight behaviour of R975 (grey dashed circles). (D) Close-up sections of 6V9X (green) and 6PQQ (red) showing S1, S4, S5, TRPL and S6, aligned on S4 emphasising the positional changes going from closed (red) to open (green). (E) Key residues identified by mutual information (only the 6V9X structure shown for clarity). K671 exhibits strong mutual information with K988 in the pocket- and pore-open simulations (green arrow), but stronger with K1001 in the pocket-closed pore-closed structure (red arrow).

Back to article page