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- W2495295145 abstract "Voltage-gated potassium (Kv) channels control K+ permeation in excitable cells. Kv channels are tetramers of α subunit, each composed of six transmembrane segments (S1-S6). The S5, P-loop and the S6 segments form the channel's permeation pathway. At the inner end of the S6, an intracellular gate opens or closes in response to voltage. A valine to cysteine mutation at position 476, near the gate, traps the mutant channel in the open state when Cd2+ is added intracellularly. It has been previously shown that four metal bridges are formed between the cysteine at position 476 of one subunit and a native histidine at position 486 in an adjacent subunit. To understand the contribution of individual bridges, we constructed a concatemer Kv channel with all subunits linked at the DNA level. After introducing the mutation V476C, ionic currents were measured using excised inside-out patches to access the intracellular part of the channel. In the absence of Cd2+, V476C concatemer mutants open and close normally. In the presence of Cd2+, successive addition of V476C mutations to the subunits of the concatemer increasingly slowed down the closing of the channel at −120 mV. With all four V476C mutations, channels are locked open with Cd2+." @default.
- W2495295145 created "2016-08-23" @default.
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- W2495295145 date "2016-02-01" @default.
- W2495295145 modified "2023-09-27" @default.
- W2495295145 title "Multiple Metal Bridges at the Intracellular Gate of a Voltage Activated Potassium Channel Prevent Closing" @default.
- W2495295145 doi "https://doi.org/10.1016/j.bpj.2015.11.3212" @default.
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