Figure 5. The residues Cys621, Glu625 and Tyr 658 in the channel
coupling domain critical for DNFB binding. (a) Representative bound
conformations of DNFB confined to the pocket consisting of three short
helixes (H2, H4 and H5) in the coupling domain in the side view (left)
and the top-down view (right). (b) Local view of a DNFB and a TRPA1
subunit interactions from hydrogen bonds (green), π-Alkyl (pink) and
π-sulfur (black) are shown as dotted lines. Halogen bond is circled in
red. (c-g) Representative current traces of wild type mouse TRPA1 (c),
C621G (d), E625A (e),
Y658A
(f) and E681A (g) mutants expressed in HEK293 cells in responses to DNFB
and AITC. (h) Summary for normalized WT TRPA1 or mutant channel current
activation by 10 µM DNFB and 300 µM AITC, shown by ratio of DNFB current
to AITC current (n = 5). Data are shown as the mean ± SEM.
*P< 0.05, ***P< 0.001, by unpairedt -test.