Matches in SemOpenAlex for { <https://semopenalex.org/work/W2556161029> ?p ?o ?g. }
- W2556161029 abstract "Significance Vesicular monoamine transporters (VMATs) are the targets of numerous psychoactive drugs, and play a critical role in the overall process of synaptic transmission by replenishing depleted monoamine stores in synaptic vesicles. VMATs transport monoamines in a process that involves exchange of two H + per substrate. Here we show that two potent inhibitors of VMAT2, tetrabenazine and reserpine, bind to different conformations of the protein. The transition that generates a reserpine-binding site requires a proton gradient across the membrane. Here we emulate the effect of the proton gradient by tinkering with residues that form the cytoplasmic gate. These findings provide vital information about the conformational dynamics of a mammalian H + -coupled antiporter. Such conformational transitions constitute essential steps in all transport processes." @default.
- W2556161029 created "2016-11-30" @default.
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- W2556161029 date "2016-11-07" @default.
- W2556161029 modified "2023-10-12" @default.
- W2556161029 title "Emulating proton-induced conformational changes in the vesicular monoamine transporter VMAT2 by mutagenesis" @default.
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- W2556161029 doi "https://doi.org/10.1073/pnas.1605162113" @default.
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