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.
Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Publishing Authors By Initials
Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Biophysical journal
VOLUME: 92
Page Numbers: 4335-43
Journal Abbreviation: Biophys. J.
ISSN: 0006-3495
DAY: 23
MONTH: 03
YEAR: 2007
Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 370626
Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Keywords Mesh Terms:
KEYWORDS: Viral Matrix Proteins
MESH TERMS: ultrastructure
Chemical & Substance for Abstract: Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Information
Substance Name: Amantadine
Registry Number: 768-94-5
Grant and Affiliation Information for Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus.
AFFILIATION: The National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Country: United States
AGENCY: United States NIAID
GRANT: R01-AI23007
ACRONYM: AI
MEDLINETA: Biophys J
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