2LJB
Structure of the influenza AM2-BM2 chimeric channel
Summary for 2LJB
| Entry DOI | 10.2210/pdb2ljb/pdb |
| Related | 2KIH 2KIX 2KWX 2LJC 2RLF |
| NMR Information | BMRB: 17928 |
| Descriptor | M2 protein, BM2 protein chimera (1 entity in total) |
| Functional Keywords | m2 channel, transport protein |
| Biological source | Influenza A virus, Influenza B virus |
| Total number of polymer chains | 4 |
| Total formula weight | 15221.48 |
| Authors | Pielak, R.M.,Oxenoid, K.,Chou, J.J. (deposition date: 2011-09-10, release date: 2011-11-16, Last modification date: 2024-05-15) |
| Primary citation | Pielak, R.M.,Oxenoid, K.,Chou, J.J. Structural investigation of rimantadine inhibition of the AM2-BM2 chimera channel of influenza viruses. Structure, 19:1655-1663, 2011 Cited by PubMed Abstract: The M2 channel of influenza A is a target of the adamantane family antiviral drugs. Two different drug-binding sites have been reported: one inside the pore, and the other is a lipid-facing pocket. A previous study showed that a chimera of M2 variants from influenza A and B that contains only the pore-binding site is sensitive to amantadine inhibition, suggesting that the primary site of inhibition is inside the pore. To obtain atomic details of channel-drug interaction, we determined the structures of the chimeric channel with and without rimantadine. Inside the channel and near the N-terminal end, methyl groups of Val27 and Ala30 from four subunits form a hydrophobic pocket around the adamantane, and the drug amino group appears to be in polar contact with the backbone oxygen of Ala30. The structures also reveal differences between the drug-bound and -unbound states of the channel that can explain drug resistance. PubMed: 22078564DOI: 10.1016/j.str.2011.09.003 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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