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Scientia Pharmaceutica is published by MDPI from Volume 84 Issue 3 (2015). Articles in this Issue were published by another publisher in Open Access under a CC-BY (or CC-BY-NC-ND) licence. Articles are hosted by MDPI on as a courtesy and upon agreement with Austrian Pharmaceutical Society (Österreichische Pharmazeutische Gesellschaft, ÖPhG).
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Sci. Pharm. 2009, 77(Posters (PO)), 205; (registering DOI)

Docking of Multiple Ligands into a New Homology Model of the Serotonin Transporter

Department of Medicinal Chemistry, University of Vienna, Althanstraße 14, 1090 Wien, Austria
Department of Pharmacology, Medical University of Vienna, Währingerstrße 13a, 1090 Wien, Austria
Author to whom correspondence should be addressed.
Received: 16 April 2009 / Accepted: 16 April 2009 / Published: 16 April 2009
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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,, 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.
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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WEISSENSTEINER, R.; SITTE, H.H.; FREISSMUTH, M.; ECKER, G.F. Docking of Multiple Ligands into a New Homology Model of the Serotonin Transporter. Sci. Pharm. 2009, 77, 205.

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