tetano
Editor, Senior Moderator
Curr Opin Virol. 2012 Apr;2(2):128-33. Epub 2012 Feb 16.
M2 protein from Influenza A: from multiple structures to biophysical and functional insights.
Cross TA, Dong H, Sharma M, Busath DD, Zhou HX.
Source
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, United States; Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, United States; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310, United States.
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.
Copyright ? 2012 Elsevier B.V. All rights reserved.
PMID:
22482709
[PubMed - in process]
PMCID:
PMC3322387
[Available on 2013/4/1]
http://www.ncbi.nlm.nih.gov/pubmed/22482709
M2 protein from Influenza A: from multiple structures to biophysical and functional insights.
Cross TA, Dong H, Sharma M, Busath DD, Zhou HX.
Source
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL 32306, United States; Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, United States; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310, United States.
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.
Copyright ? 2012 Elsevier B.V. All rights reserved.
PMID:
22482709
[PubMed - in process]
PMCID:
PMC3322387
[Available on 2013/4/1]
http://www.ncbi.nlm.nih.gov/pubmed/22482709