Identification of Intrahelical Bifurcated H-Bonds as a New Type of Gate in K⁺ Channels.

ABSTRACT: Gating of ion channels is based on structural transitions between open and closed states. To uncover the chemical basis of individual gates, we performed a comparative experimental and computational analysis between two K⁺ channels, Kcv_S and Kcv_NTS. These small viral encoded K⁺ channel proteins, with a monomer size of only 82 amino acids, resemble the pore module of all complex K⁺ channels in terms of structure and function. Even though both proteins share about 90% amino acid sequence identity, they exhibit different open probabilities with ca. 90% in Kcv_NTS and 40% in Kcv_S. Single channel analysis, mutational studies and molecular dynamics simulations show that the difference in open probability is caused by one

SUBMITTER: Rauh O 

PROVIDER: S-EPMC6638992 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature