Ion-binding properties of a K+ channel selectivity filter in different conformations

Ion-binding properties of the ClC chloride selectivity filter.

The ClC channels are members of a large protein family of chloride (Cl-) channels and secondary active Cl- transporters. Despite their diverse functions, the transmembrane architecture within the family is conserved. Here we present a crystallographic study on the ion-binding properties of the ClC selectivity filter in the close homolog from Escherichia coli (EcClC). The ClC selectivity filter ...

A minimalist model for ion partitioning and competition in a K+ channel selectivity filter

In the recent collection of articles in Perspectives on: Ion selectivity, several authors summarized the current state of knowledge on ion channel selectivity, predominated by experimental and theoretical approaches to understanding K + /Na + discrimination of passive ion channels. Considerable insight has been gained by complementary analyses of crystal structures as well as by molecular simul...

Thermodynamics of ion selectivity in the KcsA K+ channel

Initial steps of inactivation at the K+ channel selectivity filter.

K(+) efflux through K(+) channels can be controlled by C-type inactivation, which is thought to arise from a conformational change near the channel's selectivity filter. Inactivation is modulated by ion binding near the selectivity filter; however, the molecular forces that initiate inactivation remain unclear. We probe these driving forces by electrophysiology and molecular simulation of MthK,...

An Ingenious Filter: the Structural Basis for Ion Channel Selectivity

channel from Streptomyces lividans, was readily overex-pressed in bacteria (Schrempf et al., 1995). Its primary sequence is related to the class of ion-selective channels called inwardly rectifying channels, as evidenced by the presence of two putative transmembrane helices with the ion selectivity–determining P region residing Neurobiology has taken a giant step forward: we know, between them ...