Open and Closed Structures of a Barium-Blocked Potassium Channel.

ABSTRACT: Barium (Ba²⁺) is a classic permeant blocker of potassium (K⁺) channels. The "external lock-in effect" in barium block experiments, whereby the binding of external K⁺ impedes the forward translocation of the blocker, provides a powerful avenue to investigate the selectivity of the binding sites along the pore of potassium channels. Barium block experiments show that the external lock-in site is highly selective for K⁺ over Na⁺. Wild-type KcsA was crystallized in low K⁺ conditions, and the crystals were soaked in solutions containing various concentrations of barium. Structural analysis reveals open and closed gate conformations of the KcsA channel. Anomalous diffraction experiments show that Ba²⁺ primarily binds to

SUBMITTER: Rohaim A 

PROVIDER: S-EPMC7453360 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature