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• W2047156966 endingPage "2388" @default.
• W2047156966 startingPage "2380" @default.
• W2047156966 abstract "Glutamate/Aspartate transporters cotransport three Na+ and one H+ ions with the substrate and countertransport one K+ ion. The binding sites for the substrate and two Na+ ions have been observed in the crystal structure of the archeal homolog GltPh, while the binding site for the third Na+ ion has been proposed from computational studies and confirmed by experiments. Here we perform detailed free energy simulations of GltPh, giving a comprehensive characterization of the substrate and ion binding sites, and calculating their binding free energies in various configurations. Our results show unequivocally that the substrate binds after the binding of two Na+ ions. They also shed light into Asp/Glu selectivity of GltPh, which is not observed in eukaryotic glutamate transporters." @default.
• W2047156966 created "2016-06-24" @default.
• W2047156966 creator A5026255015 @default.
• W2047156966 creator A5081678489 @default.
• W2047156966 creator A5086203518 @default.
• W2047156966 date "2011-11-01" @default.
• W2047156966 modified "2023-09-26" @default.
• W2047156966 title "Free Energy Simulations of Ligand Binding to the Aspartate Transporter GltPh" @default.
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• W2047156966 doi "https://doi.org/10.1016/j.bpj.2011.10.010" @default.
• W2047156966 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3218339" @default.
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• W2047156966 hasPublicationYear "2011" @default.
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