The high-affinity binding site for tricyclic antidepressants resides in the outer vestibule of the serotonin transporter

@inproceedings{Sarker2010TheHB,
  title={The high-affinity binding site for tricyclic antidepressants resides in the outer vestibule of the serotonin transporter},
  author={Subhodeep Sarker and Rene Weissensteiner and Ilka M Steiner and Harald H. Sitte and Gerhard F. Ecker and Michael Freissmuth and Sonja Sucic},
  booktitle={Molecular pharmacology},
  year={2010}
}
The structure of the bacterial leucine transporter from Aquifex aeolicus (LeuT(Aa)) has been used as a model for mammalian Na(+)/Cl(-)-dependent transporters, in particular the serotonin transporter (SERT). The crystal structure of LeuT(Aa) liganded to tricyclic antidepressants predicts simultaneous binding of inhibitor and substrate. This is incompatible with the mutually competitive inhibition of substrates and inhibitors of SERT. We explored the binding modes of tricyclic antidepressants by… CONTINUE READING
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