2H95
Structure of the Amantadine-Blocked Influenza A M2 Proton Channel Trans-membrane Domain by Solid-state NMR spectroscopy
Summary for 2H95
| Entry DOI | 10.2210/pdb2h95/pdb |
| Descriptor | Matrix protein 2 (1 entity in total) |
| Functional Keywords | alpha helix, protein-ligand, membrane protein |
| Cellular location | Virion membrane (By similarity): P35938 |
| Total number of polymer chains | 4 |
| Total formula weight | 7833.98 |
| Authors | Hu, J.,Asbury, T.,Cross, T.A. (deposition date: 2006-06-08, release date: 2007-04-24, Last modification date: 2024-05-29) |
| Primary citation | 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 Cited by 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: 17384070DOI: 10.1529/biophysj.106.090183 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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