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

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 degrees -38 degrees ). The binding of the channel inhibitor, amantadine, results in no change in the backbone structure at position Val(27,28), which is thought to be a potential binding site for the inhibitor.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Song Z,Kovacs FA,Wang J,Denny JK,Shekar SC,Quine JR,Cross TA

doi

10.1016/S0006-3495(00)76334-X

subject

Has Abstract

pub_date

2000-08-01 00:00:00

pages

767-75

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(00)76334-X

journal_volume

79

pub_type

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