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2LJB

Structure of the influenza AM2-BM2 chimeric channel

Summary for 2LJB
Entry DOI10.2210/pdb2ljb/pdb
Related2KIH 2KIX 2KWX 2LJC 2RLF
NMR InformationBMRB: 17928
DescriptorM2 protein, BM2 protein chimera (1 entity in total)
Functional Keywordsm2 channel, transport protein
Biological sourceInfluenza A virus, Influenza B virus
Total number of polymer chains4
Total formula weight15221.48
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 citationPielak, 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: 22078564
DOI: 10.1016/j.str.2011.09.003
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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