Download MendeleyBackbone structure of the amantadine-blocked trans-membrane domain m2 proton channel from influenza a virus.
Hu, J., Asbury, T., Achuthan, S., Li, C., Bertram, R., Quine, J.R., Fu, R., Cross, T.A.(2007) Biophys J 92: 4335-4343
- PubMed: 17384070
- DOI: https://doi.org/10.1529/biophysj.106.090183
- Primary Citation of Related Structures:
2H95 - PubMed Abstract:
Amantadine is known to block the M2 proton channel of the Influenza A virus. Here, we present a structure of the M2 trans-membrane domain blocked with amantadine, built using orientational constraints obtained from solid-state NMR polarization-inversion-spin-exchange-at-the-magic-angle experiments. The data indicates a kink in the monomer between two helical fragments having 20 degrees and 31 degrees tilt angles with respect to the membrane normal. This monomer structure is then used to construct a plausible model of the tetrameric amantadine-blocked M2 trans-membrane channel. The influence of amantadine binding through comparative cross polarization magic-angle spinning spectra was also observed. In addition, spectra are shown of the amantadine-resistant mutant, S31N, in the presence and absence of amantadine.
Organizational Affiliation:
The National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
