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

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 J

journal_title

Biophysical journal

authors

Hu J,Asbury T,Achuthan S,Li C,Bertram R,Quine JR,Fu R,Cross TA

doi

10.1529/biophysj.106.090183

subject

Has Abstract

pub_date

2007-06-15 00:00:00

pages

4335-43

issue

12

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(07)71234-1

journal_volume

92

pub_type

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