期刊
CURRENT OPINION IN VIROLOGY
卷 2, 期 2, 页码 128-133出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.coviro.2012.01.005
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资金
- National Institutes of Health [AI-023007]
- National Science Foundation [0654118]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [0654118] Funding Source: National Science Foundation
The M2 protein from influenza A is a proton channel as a tetramer, with a single transmembrane helix from each monomer lining the pore. Val27 and Trp41 form gates at either end of the pore and His37 mediates the shuttling of protons across a central barrier between the N-terminal and C-terminal aqueous pore regions. Numerous structures of this transmembrane domain and of a longer construct that includes an amphipathic helix are now in the Protein Data Bank. Many structural differences are apparent from samples obtained in a variety of membrane mimetic environments. High-resolution structural results in lipid bilayers have provided novel insights into the functional mechanism of the unique HxxxW cluster in the M2 proton channel.
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