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- W2070583248 abstract "Monoamine transporters are a key feature in controlling interneuron communication by facilitating the reuptake of neurotransmitters such as dopamine, serotonin, and norepinephrine. These reuptake transporters have been computationally studied primarily through the use of homology modeling to the structurally related bacterial LeuT structure or by direct simulations of LeuT. It is thought that finding the different conformations of LeuT will aid in elucidating the mechanism of transport. To this end, a conformational sampling of LeuT was done by performing accelerated molecular dynamics (aMD) simulations on a biological membrane and an embedded LeuT transporter with different combinations of the leucine substrate and bound sodium ions. Conformational clusters were found by applying principal component analysis resulting in seven distinct structures. Both the seven structures and the entire trajectories were studied by looking at specific residues, transmembrane helical domain positions and interactions, and solvent accessibility." @default.
- W2070583248 created "2016-06-24" @default.
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- W2070583248 date "2014-01-01" @default.
- W2070583248 modified "2023-09-28" @default.
- W2070583248 title "Analyzing a Conformational Sampling of LeuT from Accelerated Molecular Dynamics Simulations" @default.
- W2070583248 doi "https://doi.org/10.1016/j.bpj.2013.11.2067" @default.
- W2070583248 hasPublicationYear "2014" @default.
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