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Comparative study of the energetics of ion permeation in Kv1.2 and KcsA potassium channels.


ABSTRACT: Biological ion channels rely on a multi-ion transport mechanism for fast yet selective permeation of ions. The crystal structure of the KcsA potassium channel provided the first microscopic picture of this process. A similar mechanism is assumed to operate in all potassium channels, but the validity of this assumption has not been well investigated. Here, we examine the energetics of ion permeation in Shaker Kv1.2 and KcsA channels, which exemplify the six-transmembrane voltage-gated and two-transmembrane inward-rectifier channels. We study the feasibility of binding a third ion to the filter and the concerted motion of ions in the channel by constructing the potential of mean force for K(+) ions in various configurations. For both channels, we find that a pair of K(+) ions can move almost

SUBMITTER: Bastug T 

PROVIDER: S-EPMC3030241 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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