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.
Highlights
The serotonin transporter (SERT) is a presynaptic membrane protein that terminates neuronal transmission of serotonin (5HT) by transporting its substrate into the emitting neuron
Leucine Transporter (LeuT) is a bacterial sodium dependent amino acid transporter, which is a homologue of the mammalian neurotransmitter sodium symporter (NSS) family, such as SERT
Basis setting of the docking parameters was achieved by redocking experiments of Trp into LeuT by using the software package MOE (Chemical Computing Group, www.chemcomp.com)
Summary
The serotonin transporter (SERT) is a presynaptic membrane protein that terminates neuronal transmission of serotonin (5HT) by transporting its substrate into the emitting neuron. Docking of Multiple Ligands into a New Homology Model of the Serotonin Transporter Austria 2 Department of Pharmacology, Medical University of Vienna, Währingerstrße 13a, 1090 Wien, Austria
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