Article
Mutations stabilizing an open conformation within the external region of the permeation pathway of the potassium channel KcsA.
European biophysics journal : EBJ - 1 Sept 2001
Meuser D, Splitt H, Wagner R, Schrempf H
Abstract excerpt
Four subunits of the bacterial Streptomyces lividans protein KcsA form a K+ channel which can be functionally reconstituted in vitro. Here we show that substitution of the tyrosine residue 82 by cysteine, valine or threonine, but not by glycine, led to functional channel types. Like the wild-type (WT) and an L81C channel, the mutant channels exhibit an internal pH-sensitive side and are cation selective. Based on...
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