How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain.

ABSTRACT: The nature of voltage sensing by voltage-activated ion channels is a key problem in membrane protein structural biology. The way in which the voltage-sensor (VS) domain interacts with its membrane environment remains unclear. In particular, the known structures of Kv channels do not readily explain how a positively charged S4 helix is able to stably span a lipid bilayer. Extended (2 x 50 ns) molecular dynamics simulations of the high-resolution structure of the isolated VS domain from the archaebacterial potassium channel KvAP, embedded in zwitterionic and in anionic lipid bilayers, have been used to explore VS/lipid interactions at atomic resolution. The simulations reveal penetration of water into the center of the VS and bilayer. Furthermore, there is significant local deformation of th

SUBMITTER: Sands ZA 

PROVIDER: S-EPMC1885962 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature