Transverse relaxation dispersion of the p7 membrane channel from hepatitis C virus reveals conformational breathing.

ABSTRACT: The p7 membrane protein encoded by hepatitis C virus (HCV) assembles into a homo-hexamer that selectively conducts cations. An earlier solution NMR structure of the hexameric complex revealed a funnel-like architecture and suggests that a ring of conserved asparagines near the narrow end of the funnel are important for cation interaction. NMR based drug-binding experiments also suggest that rimantadine can allosterically inhibit ion conduction via a molecular wedge mechanism. These results suggest the presence of dilation and contraction of the funnel tip that are important for channel activity and that the action of the drug is attenuating this motion. Here, we determined the conformational dynamics and solvent accessibility of the p7 channel. The proton exchange measurements show that th

SUBMITTER: Dev J 

PROVIDER: S-EPMC4398636 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature