Extended Data Fig. 5: Structural changes induced by Ebio1.
From: A small-molecule activation mechanism that directly opens the KCNQ2 channel
a, The VSD structure of the Ebio1-bound KCNQ2. Only the S2-S4 helices are shown for clarity. The side chain of gating charges in S4 and the gating charge transfer center residue are shown in sticks and spheres. b, Comparison of Ebio1-bound VSD of KCNQ2 with open-state VSD of KCNQ2 (PDB code: 7CR0)24 and intermediate-state VSD of KCNQ1 (PDB code: 6MIE)33, which colored cyan, gray and purple, respectively. The side chain of gating charges in S4 and the gating charge transfer center residue are shown in sticks. c, Conformational change of the KCNQ2 channel complex in one KCNQ2-CaM subunit after Ebio1 bound. The conserved ‘EKR’ motif is colored red, which undergo structural rearrangement from a loop to a helix. S6 and HA helices of KCNQ2 are colored cyan. CaM is shown as helix and surface with its N-lobe in purple and C-lobe in pink. The rotational motion of CaM after Ebio1 bound is represented by a cartoon with a dash arrow.
