Ontology highlight
ABSTRACT:
SUBMITTER: Rauh O
PROVIDER: S-EPMC6638992 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Rauh Oliver O Urban Martin M Henkes Leonhard M LM Winterstein Tobias T Greiner Timo T Van Etten James L JL Moroni Anna A Kast Stefan M SM Thiel Gerhard G Schroeder Indra I
Journal of the American Chemical Society 20170523 22
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<sup>+</sup> channels, Kcv<sub>S</sub> and Kcv<sub>NTS</sub>. These small viral encoded K<sup>+</sup> channel proteins, with a monomer size of only 82 amino acids, resemble the pore module of all complex K<sup>+</sup> channels in terms of structure and function. Even though both ...[more]