5C02
Influenza A M2 transmembrane domain drug-resistant S31N mutant at pH 8.0
Summary for 5C02
| Entry DOI | 10.2210/pdb5c02/pdb |
| Descriptor | Matrix protein 2, STRONTIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | membrane protein, influenza, drug resistance |
| Biological source | Influenza A virus (A/Udorn/307/1972(H3N2)) |
| Total number of polymer chains | 1 |
| Total formula weight | 3693.05 |
| Authors | Thomaston, J.L.,DeGrado, W.F. (deposition date: 2015-06-12, release date: 2016-05-04, Last modification date: 2024-11-13) |
| Primary citation | Thomaston, J.L.,DeGrado, W.F. Crystal structure of the drug-resistant S31N influenza M2 proton channel. Protein Sci., 25:1551-1554, 2016 Cited by PubMed Abstract: The M2 protein is a small proton channel found in the influenza A virus that is necessary for viral replication. The M2 channel is the target of a class of drugs called the adamantanes, which block the channel pore and prevent the virus from replicating. In recent decades mutations have arisen in M2 that prevent the adamantanes from binding to the channel pore, with the most prevalent of these mutations being S31N. Here we report the first crystal structure of the S31N mutant crystallized using lipidic cubic phase crystallization techniques and solved to 1.59 Å resolution. The Asn31 residues point directly into the center of the channel pore and form a hydrogen-bonded network that disrupts the drug-binding site. Ordered waters in the channel pore form a continuous hydrogen bonding network from Gly34 to His37. PubMed: 27082171DOI: 10.1002/pro.2937 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.591 Å) |
Structure validation
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