Abstract
The serotonin transporter (SERT) is a presynaptic membrane protein that terminates neuronal transmission of serotonin (5HT) by transporting its substrate into the emitting neuron. Recently new crystal structures of the Leucine Transporter (LeuT) with multiple bound ligands have been published [1]. LeuT is a bacterial sodium dependent amino acid transporter, which is a homologue of the mammalian neurotransmitter sodium symporter (NSS) family (tcdb-code 2.A.22, www.tcdb.org), such as SERT. In light of our studies on the molecular basis of inhibitor binding we constructed a new homology model of SERT and used this for docking studies of a series of pharmacologically active ligands.