Common mechanism of pore opening shared by five different potassium channels.

ABSTRACT: A fundamental question associated with the function of ion channels is the conformational changes that allow for reversibly opening/occluding the pore through which the cations permeate. The recently elucidated crystal structures of potassium channels reveal similar structural motifs at their pore-forming regions, suggesting that they share a common gating mechanism. The validity of this hypothesis is explored by analyzing the collective dynamics of five known K(+) channel structures. Normal-mode analysis using the Gaussian network model strikingly reveals that all five structures display the same intrinsic motions at their pore-forming region despite the differences in their sequences, structures, and activation mechanisms. Superposition of the most cooperative mode profiles shows that th

SUBMITTER: Shrivastava IH 

PROVIDER: S-EPMC1459499 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature