Skip to main navigation Skip to search Skip to main content

Homology modeling of the serotonin transporter: Insights into the primary escitalopram-binding Site

  • Anne Marie Jørgensen
  • , L. Tagmose
  • , A.M.M. Jørgensen
  • , S. Topiol
  • , M. Sabio
  • , K. Gundertofte
  • , K.P. Bøgesø
  • , Günther H.j. Peters
  • H. Lundbeck A/S
  • Lundbeck US

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

The serotonin transporter (SERT) is one of the neurotransmitter transporters that plays a critical role in the regulation of endogenous amine concentrations and therefore is an important target for therapeutic agents affecting the central nervous system. The recently published, high resolution X-ray structure of the closely related amino acid transporter, Aquifex aeolicus leucine transporter (LeuT), provides an opportunity to develop a three-dimensional model of the structure of SERT. We present herein a homology model of SERT using LeuT as the template and containing escitalopram as a bound ligand. Our model explains selectivities known from mutational studies and varying ligand data, which are discussed and illustrated in the paper.
Original languageEnglish
JournalChemMedChem
Volume2
Issue number6
Pages (from-to)815-826
Number of pages12
ISSN1860-7179
DOIs
Publication statusPublished - 2007

Keywords

  • Escitalopram
  • Homology modeling
  • Molecular recognition
  • Serotonin transporter
  • Structure–activity relationships

Fingerprint

Dive into the research topics of 'Homology modeling of the serotonin transporter: Insights into the primary escitalopram-binding Site'. Together they form a unique fingerprint.

Cite this