Journal
BIOPHYSICAL JOURNAL
Volume 92, Issue 12, Pages 4335-4343Publisher
CELL PRESS
DOI: 10.1529/biophysj.106.090183
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Funding
- NIAID NIH HHS [R01-AI23007, R01 AI023007, R01 AI073891] Funding Source: Medline
- NIGMS NIH HHS [P01 GM064676, P01-GM064676] Funding Source: Medline
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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.
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