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...
| मुख्य लेखकों: | , , , |
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| अन्य लेखक: | |
| स्वरूप: | लेख |
| भाषा: | en_US |
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American Chemical Society (ACS)
2013
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| ऑनलाइन पहुंच: | http://hdl.handle.net/1721.1/82075 https://orcid.org/0000-0002-3349-6212 https://orcid.org/0000-0003-1589-832X |
| _version_ | 1826208952819384320 |
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| author | Chou, James J. Andreas, Loren Eddy, Matthew Thomas Griffin, Robert Guy |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Chou, James J. Andreas, Loren Eddy, Matthew Thomas Griffin, Robert Guy |
| author_sort | Chou, James J. |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T14:15:21Z |
| format | Article |
| id | mit-1721.1/82075 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:15:21Z |
| publishDate | 2013 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/820752022-10-01T20:07:07Z Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A Chou, James J. Andreas, Loren Eddy, Matthew Thomas Griffin, Robert Guy Massachusetts Institute of Technology. Department of Chemistry Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology) Andreas, Loren Eddy, Matthew Thomas Griffin, Robert Guy 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. National Institutes of Health (U.S.) (Grant EB-001960) National Institutes of Health (U.S.) (Grant EB-002026) National Institutes of Health (U.S.) (Grant AI-067438) National Institutes of Health (U.S.) (Grant GM-094608) 2013-11-12T13:34:21Z 2013-11-12T13:34:21Z 2012-04 2012-01 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 http://hdl.handle.net/1721.1/82075 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. https://orcid.org/0000-0002-3349-6212 https://orcid.org/0000-0003-1589-832X en_US http://dx.doi.org/10.1021/ja3003606 Journal of the American Chemical Society Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society (ACS) PMC |
| spellingShingle | Chou, James J. Andreas, Loren Eddy, Matthew Thomas Griffin, Robert Guy Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A |
| title | Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A |
| title_full | Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A |
| title_fullStr | Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A |
| title_full_unstemmed | Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A |
| title_short | Magic-Angle-Spinning NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A |
| title_sort | magic angle spinning nmr of the drug resistant s31n m2 proton transporter from influenza a |
| url | http://hdl.handle.net/1721.1/82075 https://orcid.org/0000-0002-3349-6212 https://orcid.org/0000-0003-1589-832X |
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