How LeuT shapes our understanding of the mechanisms of sodium‐coupled neurotransmitter transporters
- 23 August 2013
- journal article
- review article
- Published by Wiley in Journal Of Physiology-London
- Vol. 592 (5), 863-869
- https://doi.org/10.1113/jphysiol.2013.259051
Abstract
Neurotransmitter transporters are ion-coupled symporters that drive the uptake of neurotransmitters from the synapse. In the past decade, the structure of a bacterial amino acid transporter, LeuT has given valuable insights into understanding the architecture and mechanism of mammalian neurotransmitter transporters. Different conformations of LeuT that include a substrate-free state, inward-open state, competitive and non-competitive inhibitor bound states have revealed a mechanistic frame work 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.Keywords
Funding Information
- American Heart Association (11POST7370096)
- Howard Hughes Medical Institute
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