Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A
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 spect...
| Main Authors: | , , , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
American Chemical Society (ACS)
2013
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| Online Access: | http://hdl.handle.net/1721.1/82075 https://orcid.org/0000-0002-3349-6212 https://orcid.org/0000-0003-1589-832X |
| Summary: | 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. |
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