Calmodulin (CaM) binding to the AB module is critical for multiple mechanisms governing the function of Kv7.2 potassium subunits, which are one of the main components of the non-inactivating K+ M-current, a key controller of neuronal excitability. Structural analysis indicates that the CaM N-lobe engages with helix B, whereas the C-lobe anchors to the IQ site within helix A. Here we report the identification of a novel site between helices A and B that assist in CaM binding, whose sequence is reminiscent of the TW helix within the CaM C-lobe anchoring site of SK2 K+ channels. Mutations that disrupt CaM binding within the TW site, helix B, or helix A yield functional channels, whereas no function is observed when the TW site and helix A, or the TW site and helix B are mutated simultaneously. Our data indicate that the TW is dispensable for function, contributes to the stabilization of the CaM/Kv7.2 complex, and becomes essential when docking to either helix A or helix B is perturbed.