1MP6
Structure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopy
Summary for 1MP6
| Entry DOI | 10.2210/pdb1mp6/pdb |
| Descriptor | Matrix protein M2 (1 entity in total) |
| Functional Keywords | influenza a virus, membrane protein structure, m2 proton channel, solid state nmr, membrane protein |
| Total number of polymer chains | 1 |
| Total formula weight | 2730.30 |
| Authors | Wang, J.,Kim, S.,Kovacs, F.,Cross, T.A. (deposition date: 2002-09-11, release date: 2002-09-25, Last modification date: 2024-05-22) |
| Primary citation | Wang, J.,Kim, S.,Kovacs, F.,Cross, T.A. Structure of the transmembrane region of the M2 protein H(+) channel. Protein Sci., 10:2241-2250, 2001 Cited by PubMed Abstract: The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high-resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid-state NMR. With this unique information, the tetrameric structure of this H(+) channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle. PubMed: 11604531DOI: 10.1110/ps.17901 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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