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- W2148618424 abstract "The M2 protein, a proton channel, from Influenza A has been structurally characterized by X-ray diffraction and by solution and solid-state NMR spectroscopy in a variety of membrane mimetic environments. These structures show substantial backbone differences even though they all present a left-handed tetrameric helical bundle for the transmembrane domain. Variations in the helix tilt influence drug binding and the chemistry of the histidine tetrad responsible for acid activation, proton selectivity and transport. Some of the major structural differences do not arise from the lack of precision, but instead can be traced to the influences of the membrane mimetic environments. The structure in lipid bilayers displays unique chemistry for the histidine tetrad, which binds two protons cooperatively to form a pair of imidazole-imidazolium dimers. The resulting interhistidine hydrogen bonds contribute to a three orders of magnitude enhancement in tetramer stability. Integration with computation has provided detailed understanding of the functional mechanism for proton selectivity, conductance and gating of this important drug target." @default.
- W2148618424 created "2016-06-24" @default.
- W2148618424 creator A5046197938 @default.
- W2148618424 creator A5075658290 @default.
- W2148618424 date "2013-03-01" @default.
- W2148618424 modified "2023-10-01" @default.
- W2148618424 title "Modeling the membrane environment has implications for membrane protein structure and function: Influenza A M2 protein" @default.
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- W2148618424 doi "https://doi.org/10.1002/pro.2232" @default.
- W2148618424 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3610044" @default.
- W2148618424 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23389890" @default.
- W2148618424 hasPublicationYear "2013" @default.
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