Figure 5
From: Open conformation of hERG channel turrets revealed by a specific scorpion toxin BmKKx2
Effects of the turret and pore region residues of hERG channel on BmKKx2 binding affinity. (A-P) Representative current traces of hERG channel mutants showing current blocks by BmKKx2. (A) hERG-R582A, (B) hERG-I583A, (C) hERG-L586A, (D) hERG-H587A, (E) hERG-N588A, (F) hERG-D591A, (G) hERG-Q592A, (H) hERG-K595A, (I) hERG-P596A, (J) hERG-Y597A, (K) hERG-N598A, (L) hERG-S600A, (M) hERG-K608A, (N) hERG-K610A, (O) hERG-T613A and (P) hERG-S631A.