Structural highlights
Publication Abstract from PubMed
Amantadine is known to block the M2 proton channel of the Influenza A virus. Here, we present a structure of the M2 trans-membrane domain blocked with amantadine, built using orientational constraints obtained from solid-state NMR polarization-inversion-spin-exchange-at-the-magic-angle experiments. The data indicates a kink in the monomer between two helical fragments having 20 degrees and 31 degrees tilt angles with respect to the membrane normal. This monomer structure is then used to construct a plausible model of the tetrameric amantadine-blocked M2 trans-membrane channel. The influence of amantadine binding through comparative cross polarization magic-angle spinning spectra was also observed. In addition, spectra are shown of the amantadine-resistant mutant, S31N, in the presence and absence of amantadine.
Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus.,Hu J, Asbury T, Achuthan S, Li C, Bertram R, Quine JR, Fu R, Cross TA Biophys J. 2007 Jun 15;92(12):4335-43. Epub 2007 Mar 23. PMID:17384070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hu J, Asbury T, Achuthan S, Li C, Bertram R, Quine JR, Fu R, Cross TA. Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus. Biophys J. 2007 Jun 15;92(12):4335-43. Epub 2007 Mar 23. PMID:17384070 doi:biophysj.106.090183
