2H95

Structure of the Amantadine-Blocked Influenza A M2 Proton Channel Trans-membrane Domain by Solid-state NMR spectroscopy

2H95 の概要

• エントリーDOI: 10.2210/pdb2h95/pdb
• 分子名称: Matrix protein 2 (1 entity in total)
• 機能のキーワード: alpha helix, protein-ligand, membrane protein
• 細胞内の位置: Virion membrane (By similarity): P35938
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 7833.98

構造登録者

Hu, J.,Asbury, T.,Cross, T.A. (登録日: 2006-06-08, 公開日: 2007-04-24, 最終更新日: 2024-05-29)

主引用文献

Hu, J.,Asbury, T.,Achuthan, S.,Li, C.,Bertram, R.,Quine, J.R.,Fu, R.,Cross, T.A.
Backbone structure of the amantadine-blocked trans-membrane domain m2 proton channel from influenza a virus.
Biophys.J., 92:4335-4343, 2007

PubMed Abstract: 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.

PubMed: 17384070
DOI: 10.1529/biophysj.106.090183

実験手法

SOLID-STATE NMR