Conformational changes in the selectivity filter of the open-state KcsA channel: an energy minimization study.

ABSTRACT: Potassium channels switch between closed and open conformations and selectively conduct K(+) ions. There are at least two gates. The TM2 bundle at the intracellular site is the primary gate of KcsA, and rearrangements at the selectivity filter (SF) act as the second gate. The SF blocks ion flow via an inactivation process similar to C-type inactivation of voltage-gated K(+) channels. We recently generated the open-state conformation of the KcsA channel. We found no major, possibly inactivating, structural changes in the SF associated with this massive inner-pore rearrangement, which suggests that the gates might act independently. Here we energy-minimize the open state of wild-type and mutant KcsA, validating in silico structures of energy-minimized SFs by comparison with crystallographic

SUBMITTER: Miloshevsky GV 

PROVIDER: S-EPMC2547464 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature