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How LeuT shapes our understanding of the mechanisms of sodium‐coupled neurotransmitter transporters
Author(s) -
Penmatsa Aravind,
Gouaux Eric
Publication year - 2013
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2013.259051
Subject(s) - neurotransmitter transporter , transporter , neurotransmitter , synaptic cleft , symporter , gaba transporter , reuptake , chemistry , biochemistry , biophysics , neuroscience , biology , serotonin , receptor , gene
Neurotransmitter transporters are ion‐coupled symporters that drive the uptake of neurotransmitters from neural synapses. In the past decade, the structure of a bacterial amino acid transporter, leucine transporter (LeuT), has given valuable insights into the understanding of architecture and mechanism of mammalian neurotransmitter transporters. Different conformations of LeuT, including a substrate‐free state, inward‐open state, and competitive and non‐competitive inhibitor‐bound states, have revealed a mechanistic framework for the transport and transport inhibition of neurotransmitters. The current review integrates our understanding of the mechanistic and pharmacological properties of eukaryotic neurotransmitter transporters obtained through structural snapshots of LeuT.