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 Jjournal_title
Biophysical journalauthors
Song Z,Kovacs FA,Wang J,Denny JK,Shekar SC,Quine JR,Cross TAdoi
10.1016/S0006-3495(00)76334-Xsubject
Has Abstractpub_date
2000-08-01 00:00:00pages
767-75issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(00)76334-Xjournal_volume
79pub_type
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