Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A
Author(s)Chou, James J.; Andreas, Loren; Eddy, Matthew Thomas; Griffin, Robert Guy
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We report chemical shift assignments of the drug-resistant S31N mutant of M2[subscript 18–60] determined using 3D magic-angle-spinning (MAS) NMR spectra acquired with a [superscript 15]N–[superscript 13]C ZF-TEDOR transfer followed by [superscript 13]C–[superscript 13]C mixing by RFDR. The MAS spectra reveal two sets of resonances, indicating that the tetramer assembles as a dimer of dimers, similar to the wild-type channel. Helicies from the two sets of chemical shifts are shown to be in close proximity at residue H37, and the assignments reveal a difference in the helix torsion angles, as predicted by TALOS+, for the key resistance residue N31. In contrast to wild-type M2[subscript 18–60], chemical shift changes are minimal upon addition of the inhibitor rimantadine, suggesting that the drug does not bind to S31N M2.
DepartmentFrancis Bitter National Magnet Laboratory; Massachusetts Institute of Technology. Department of Chemistry
Journal of the American Chemical Society
American Chemical Society (ACS)
Andreas, Loren B., Matthew T. Eddy, James J. Chou, and Robert G. Griffin. “Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A.” Journal of the American Chemical Society 134, no. 17 (May 2, 2012): 7215-7218.
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