Fig. 2: Interaction interfaces between KCNQ1 and KCNE1.
From: Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating
a In (KCNQ1 + KCNE1)APO structure, KCNE1 shows direct contact with three different subunits: the main subunit (main), its neighboring subunit (neighboring), and its opposite subunit (opposite). Between “main” and KCNE1: Q147/D39, Y148/K41, F130/T58, F127/L59 and H240/Y65; between “neighboring” and KCNE1: S298/E43, F270/F54, Y267/T58 and Q260/S64; between “opposite” and KCNE1: W323/E43 and S330/Y46. b In (KCNQ1 + KCNE1)PIP2 structure, KCNE1 shows direct contact with three different subunits: the main subunit (main), its neighboring subunit (neighboring), and its opposite subunit (opposite). Between “main” and KCNE1: Q147/D39, H126/M62, H126/Y65, C122/Y65, and F123/L63; between “neighboring” and KCNE1: S298/E43, L303/V47 and Y267/F54; between “opposite” and KCNE1: W323/E43 and S330/Y46. c State-dependent interactions between KCNQ1 and KCNE1 in (KCNQ1 + KCNE1)APO and (KCNQ1 + KCNE1)PIP2. Among them, four residue pairs Q147/D39, S298/E43, W323/E43 and S330/Y46, remain interacted in both (KCNQ1 + KCNE1)APO and (KCNQ1 + KCNE1)PIP2 (marked with black triangles in a, b), and are highlighted with blue and green colors, respectively.
