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Biophys J. 2007 Jun 15;92(12):4335-43. Epub 2007 Mar 23.

Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus.

Author information

1
The National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.

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.

PMID:
17384070
PMCID:
PMC1877758
DOI:
10.1529/biophysj.106.090183
[Indexed for MEDLINE]
Free PMC Article

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