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Elsevier, Current Opinion in Virology, 2(2), p. 128-133

DOI: 10.1016/j.coviro.2012.01.005

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M2 Protein from Influenza A: From multiple structures to biophysical and functional insights

Journal article published in 2012 by Timothy A. Cross, Hao Dong, Mukesh Sharma, David D. Busath, Huan-Xiang Zhou ORCID
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.