Structural properties determining low K⁺ affinity of the selectivity filter in the TWIK1 K⁺ channel.

ABSTRACT: Canonical K⁺ channels are tetrameric and highly K⁺-selective, whereas two-pore-domain K⁺ (K2P) channels form dimers, but with a similar pore architecture. A two-pore-domain potassium channel TWIK1 (KCNK1 or K2P1) allows permeation of Na⁺ and other monovalent ions, resulting mainly from the presence of Thr-118 in the P1 domain. However, the mechanistic basis for this reduced selectivity is unclear. Using ion-exchange-induced difference IR spectroscopy, we analyzed WT TWIK1 and T118I (highly K⁺-selective) and L228F (substitution in the P2 domain) TWIK1 variants and found that in the presence of K⁺ ions, WT and both variants exhibit an amide-I band at 1680 cm^-1 This band corresponds to interactions of the backbone ca

SUBMITTER: Tsukamoto H 

PROVIDER: S-EPMC5936812 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature