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• W2018010932 abstract "Significance Symporters or cotransporters are proteins that use sodium electrochemical potential gradients to drive sugars, amino acids, anions, and neurotransmitters into cells. Progress in structural biology has provided important clues about substrate binding sites, but the identification of Na + in binding sites has been a challenge owing to the high resolution required. We use a biophysical method to determine the Na + affinity of electrogenic transporters, and, together with site-directed mutagenesis, we identify the two Na + binding sites in the human intestinal Na + /glucose cotransporter SGLT1. The results provide insights into the Na + binding sites of symporters and the mechanism of active transport." @default.
• W2018010932 created "2016-06-24" @default.
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• W2018010932 date "2013-11-04" @default.
• W2018010932 modified "2023-10-13" @default.
• W2018010932 title "Functional identification and characterization of sodium binding sites in Na symporters" @default.
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• W2018010932 doi "https://doi.org/10.1073/pnas.1319218110" @default.
• W2018010932 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3839715" @default.
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