Structural interactions between lipids, water and S1-S4 voltage-sensing domains.

ABSTRACT: Membrane proteins serve crucial signaling and transport functions, yet relatively little is known about their structures in membrane environments or how lipids interact with these proteins. For voltage-activated ion channels, X-ray structures suggest that the mobile voltage-sensing S4 helix would be exposed to the membrane, and functional studies reveal that lipid modification can profoundly alter channel activity. Here, we use solid-state NMR to investigate structural interactions of lipids and water with S1-S4 voltage-sensing domains and to explore whether lipids influence the structure of the protein. Our results demonstrate that S1-S4 domains exhibit extensive interactions with lipids and that these domains are heavily hydrated when embedded in a membrane. We also find evidence for pre

SUBMITTER: Krepkiy D 

PROVIDER: S-EPMC3616881 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature