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Magic-angle-spinning NMR of the drug resistant S31N M2 proton transporter from influenza A.

ABSTRACT: We report chemical shift assignments of the drug-resistant S31N mutant of M2(18-60) determined using 3D magic-angle-spinning (MAS) NMR spectra acquired with a (15)N-(13)C ZF-TEDOR transfer followed by (13)C-(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(18-60), chemical shift changes are minimal upon addition of the inhibitor rimantadine, suggesting that the drug does not bind to S31N M2.

SUBMITTER: Andreas LB

PROVIDER: S-EPMC3342473 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Magic-angle-spinning NMR of the drug resistant S31N M2 proton transporter from influenza A.

Andreas Loren B LB Eddy Matthew T MT Chou James J JJ Griffin Robert G RG

Journal of the American Chemical Society 20120423 17

We report chemical shift assignments of the drug-resistant S31N mutant of M2(18-60) determined using 3D magic-angle-spinning (MAS) NMR spectra acquired with a (15)N-(13)C ZF-TEDOR transfer followed by (13)C-(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 dif ...[more]

PMID: 22480220

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