3BKD
High resolution Crystal structure of Transmembrane domain of M2 protein
Summary for 3BKD
| Entry DOI | 10.2210/pdb3bkd/pdb |
| Descriptor | Transmembrane Domain of Matrix protein M2, octyl beta-D-glucopyranoside, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | proton channel, m2tm, influenza a virus m2 protein, viral protein, membrane protein |
| Total number of polymer chains | 8 |
| Total formula weight | 24807.73 |
| Authors | Stouffer, A.L.,Acharya, R.,Salom, D. (deposition date: 2007-12-06, release date: 2008-01-29, Last modification date: 2024-11-20) |
| Primary citation | Stouffer, A.L.,Acharya, R.,Salom, D.,Levine, A.S.,Di Costanzo, L.,Soto, C.S.,Tereshko, V.,Nanda, V.,Stayrook, S.,DeGrado, W.F. Structural basis for the function and inhibition of an influenza virus proton channel Nature, 451:596-599, 2008 Cited by PubMed Abstract: The M2 protein from influenza A virus is a pH-activated proton channel that mediates acidification of the interior of viral particles entrapped in endosomes. M2 is the target of the anti-influenza drugs amantadine and rimantadine; recently, resistance to these drugs in humans, birds and pigs has reached more than 90% (ref. 1). Here we describe the crystal structure of the transmembrane-spanning region of the homotetrameric protein in the presence and absence of the channel-blocking drug amantadine. pH-dependent structural changes occur near a set of conserved His and Trp residues that are involved in proton gating. The drug-binding site is lined by residues that are mutated in amantadine-resistant viruses. Binding of amantadine physically occludes the pore, and might also perturb the pK(a) of the critical His residue. The structure provides a starting point for solving the problem of resistance to M2-channel blockers. PubMed: 18235504DOI: 10.1038/nature06528 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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