Transmembrane domain of M2 protein from influenza A virus studied by solid-state 15N polarization inversion spin exchange at magic angle NMR

Zhiyan Song, F. A. Kovacs, J. Wang, Jeffrey K. Denny, S. C. Shekar, J. R. Quine, T. A. Cross

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Abstract

The M2 protein from the influenza A virus forms a proton channel in the virion that is essential for infection. This tetrameric protein appears to form a four-helix bundle spanning the viral membrane. Here the solid-state NMR method, 2D polarization inversion spin exchange at magic angle (PISEMA), has been used to obtain multiple constraints from specifically amino acid-labeled samples. The improvement of spectral resolution from 2D PISEMA over 1D methods and 2D separated local field methods is substantial. The reliability of the method is validated by comparison of anisotropic chemical shift and heteronuclear dipolar interactions from single site labeled samples. The quantitative interpretation of the high-resolution constraints confirms the helix tilt to be within the range of previous experimental determinations (32°-38°). The binding of the channel inhibitor, amantadine, results in no change in the backbone structure at position Val27,28, which is thought to be a potential binding site for the inhibitor.

Original languageEnglish (US)
Pages (from-to)767-775
Number of pages9
JournalBiophysical journal
Volume79
Issue number2
DOIs
Publication statusPublished - Jan 1 2000

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ASJC Scopus subject areas

  • Biophysics

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