Voltage-sensing-domain conformational differences between open and C-type inactivated states. Side view of VSD structures and maps of Kv1.2s in (A) inactivated state. (B) Kv1.2s VSD R3/E183 (upper), R4/E226 (middle), and K5/F233 (lower) interactions in the inactivated state. VSD structure in open state. (D) VSD relative position of R2/E138 (upper) and R3/E226 (middle), K5/F233 (lower) interactions in the open state. Positively charged and negatively charged residues are shown in blue and red, while aromatic residues are shown in green. Side view (E), top view (F, upper) and bottom view (F, lower) VSD conformational difference between open (yellow) and inactivated (purple) states. Superposition of (G) Shaker open (PDB: 7SIP), Shaker W434F inactivated (PDB: 7SJ1) and (F) Kv1.2-2.1 open (PDB: 7SIZ), Kv1.2-2.1 3m inactivated (PDB: 7SIT) VSD structures. (I-L) Superposition of VSD structures. (I) Kv1.2s (yellow) and Kv1.2-2.1 (light blue, PDB: 2R9R); (J) Kv1.2s W366F (purple) and Kv1.2-2.1 V406W (carnation, PDB: 5WIE); (K) Kv1.2 (yellow) and Kv1.3 (green, PDB: 7EJ1); (L) Kv1.2 W366F (purple) and Kv1.3 H451N (clover, PDB: 7EJ2).