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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Hu J,Asbury T,Achuthan S,Li C,Bertram R,Quine JR,Fu R,Cross TAdoi
10.1529/biophysj.106.090183subject
Has Abstractpub_date
2007-06-15 00:00:00pages
4335-43issue
12eissn
0006-3495issn
1542-0086pii
S0006-3495(07)71234-1journal_volume
92pub_type
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