Fig. 2: Tripartite interactions of the Kv4.2 N terminus, Kv4.2 C terminus and KChIP1. | Nature

Fig. 2: Tripartite interactions of the Kv4.2 N terminus, Kv4.2 C terminus and KChIP1.

From: Structural basis of gating modulation of Kv4 channel complexes

Fig. 2

a, Overall structure of the Kv4.2–KChIP1 complex. The two neighbouring Kv4.2 subunits and one KChIP1 subunit are coloured yellow, red and blue, respectively. The C-terminal cytoplasmic S6 helix stops at S450 when it reaches the bottom of the complex. The interaction site of Kv4.2 and KChIP1 is highlighted by a dotted box. A magnified view from the direction of the arrow is presented in b. b, c, Comparison of the Kv4–KChIP1 complex with (b) or without (c) the Kv4 C terminus. Bottom views of the Kv4.2 (full-length)–KChIP1 complex (b) and the Kv4.3(T1)–KChIP1 complex (c; Protein Data Bank (PDB) code: 2NZ0) are shown. The neighbouring Kv4 subunits are coloured red and yellow. The Kv4.2 S6 helix (Kv4.2-S6) extends downward to the bottom of the complex (S450) and is further followed by the C-terminal segment (Kv4.2-C) consisting of a short helix and a loop (S472–D495), which occupies the hydrophobic space generated by the Kv4.2 N terminus (Kv4.2-N) and KChIP1 (b). d, Inter-subunit interaction of the Kv4.2 N and C termini. Residues involved in the interaction are shown. Two neighbouring Kv4.2 subunits are coloured red and yellow. e, Interaction of the Kv4.2 C terminus (red) and KChIP1 (blue). Residues involved in the interaction are shown. f, The Kv4.2 intracellular S6 helix is captured by KChIP1 and the Kv4.2 C terminus. Residues involved in the interaction are shown.

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