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. This article is protected by copyright. All rights reserved