Molecular determinants of interactions between the N-terminal domain and the transmembrane core that modulate hERG K+ channel gating.

ABSTRACT: A conserved eag domain in the cytoplasmic amino terminus of the human ether-a-go-go-related gene (hERG) potassium channel is critical for its slow deactivation gating. Introduction of gene fragments encoding the eag domain are able to restore normal deactivation properties of channels from which most of the amino terminus has been deleted, and also those lacking exclusively the eag domain or carrying a single point mutation in the initial residues of the N-terminus. Deactivation slowing in the presence of the recombinant domain is not observed with channels carrying a specific Y542C point mutation in the S4-S5 linker. On the other hand, mutations in some initial positions of the recombinant fragment also impair its ability to restore normal deactivation. Fluorescence resonance energy trans

SUBMITTER: Fernandez-Trillo J 

PROVIDER: S-EPMC3174182 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature