tetano
Editor, Senior Moderator
J Am Chem Soc. 2012 Apr 5. [Epub ahead of print]
MAS NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A.
Andreas LB, Eddy MT, Chou JJ, Griffin RG.
Abstract
We report chemical shift assignments of the drug-resistant S31N mutant of M218-60 determined with 3D spectra acquired with a 15N-13C ZF-TEDOR transfer followed by 13C-13C mixing by RFDR. The spectral assignments reveal two sets of resonances, indicating that the tetramer assembles as a dimer of dimers, similar to the wild type channel. The two sets of chemical shifts reveal a difference in the helix torsion angles, as predicted by TALOS+, for the key resistance residue N31. In contrast to wild type M218-60, chemical shift changes are minimal with addition of the inhibitor rimantadine, providing a negative control on the functional relevance of such changes.
PMID:
22480220
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22480220
MAS NMR of the Drug Resistant S31N M2 Proton Transporter from Influenza A.
Andreas LB, Eddy MT, Chou JJ, Griffin RG.
Abstract
We report chemical shift assignments of the drug-resistant S31N mutant of M218-60 determined with 3D spectra acquired with a 15N-13C ZF-TEDOR transfer followed by 13C-13C mixing by RFDR. The spectral assignments reveal two sets of resonances, indicating that the tetramer assembles as a dimer of dimers, similar to the wild type channel. The two sets of chemical shifts reveal a difference in the helix torsion angles, as predicted by TALOS+, for the key resistance residue N31. In contrast to wild type M218-60, chemical shift changes are minimal with addition of the inhibitor rimantadine, providing a negative control on the functional relevance of such changes.
PMID:
22480220
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22480220