Trapping the 2,4-K+-Ion Bound Configuration of KcsA's Selectivity Filter

Ion–Ion Interactions at the Selectivity Filter

In the Kv2.1 potassium channel, binding of K(+) to a high-affinity site associated with the selectivity filter modulates channel sensitivity to external TEA. In channels carrying Na(+) current, K(+) interacts with the TEA modulation site at concentrations </=30 microM. In this paper, we further characterized the TEA modulation site and examined how varying K(+) occupancy of the pore influenced ...

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 ...

Ion conduction and selectivity in K(+) channels.

Potassium (K(+)) channels are tetrameric membrane-spanning proteins that provide a selective pore for the conductance of K(+) across the cell membranes. These channels are most remarkable in their ability to discriminate K(+) from Na(+) by more than a thousandfold and conduct at a throughput rate near diffusion limit. The recent progress in the structural characterization of K(+) channel provid...

Ion Conduction and Selectivity in K+ Channels

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,...