Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer.

ABSTRACT: Voltage-dependent ion channels are fundamental to the physiology of excitable cells because they underlie the generation and propagation of the action potential and excitation-contraction coupling. To understand how ion channels work, it is important to determine their structures in different conformations in a membrane environment. The validity of the crystal structure for the prokaryotic K(+) channel, K(V)AP, has been questioned based on discrepancies with biophysical data from functional eukaryotic channels, underlining the need for independent structural data under native conditions. We investigated the structural organization of two prokaryotic voltage-gated channels, NaChBac and K(V)AP, in liposomes by using luminescence resonance energy transfer. We describe here a transmembrane pac

SUBMITTER: Richardson J 

PROVIDER: S-EPMC1635094 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature