Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Voltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in membrane voltage. We used molecular dynamics simulations to examine interactions with lipids of several VS homologs. VSs in intact channels in the activated state are exposed to phospholipids, leading to a characteristic local distortion of the lipid bilayer which decreases its thickness by ∼10 Å. This effect is mediated by a conserved hydrophilic stretch in the S4-S5 segment linking the VS and the pore domains, and may favor gating charges crossing the membrane. In cationic lipid bilayers lacking phosphate groups, VSs form fewer contacts with lipid headgroups. The S3-S4 paddle motifs show persistent interactions of individual lipid molecules, influenced by the hairpin loop. In conclusion, our results suggest common interactions with phospholipids for various VS homologs, providing insights into the molecular basis of their stabilization in the membrane and how they are altered by lipid modification.

Original publication

DOI

10.1016/j.bpj.2010.11.049

Type

Journal article

Journal

Biophys J

Publication Date

16/02/2011

Volume

100

Pages

875 - 884

Keywords

Amino Acid Motifs, Amino Acid Sequence, Animals, Conserved Sequence, Humans, Ion Channel Gating, Ion Channels, Lipid Bilayers, Molecular Dynamics Simulation, Molecular Sequence Data, Phosphates, Phospholipids, Porosity, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid