The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter

The serotonin transporter (SERT) terminates serotonin signaling and its activity is modulated by antidepressants. Here authors reveal the mechanistic details underlying the coupling between the two binding sites in SERT and a high-affinity ligand for the allosteric site.

Bibliographic Details
Main Authors: Per Plenge, Ara M. Abramyan, Gunnar Sørensen, Arne Mørk, Pia Weikop, Ulrik Gether, Benny Bang-Andersen, Lei Shi, Claus J. Loland
Format: Article
Language:English
Published: Nature Publishing Group 2020-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-15292-y
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spelling doaj-4706c23f56b542ffad3d502b3f12fe7e2021-05-11T07:58:33ZengNature Publishing GroupNature Communications2041-17232020-03-0111111210.1038/s41467-020-15292-yThe mechanism of a high-affinity allosteric inhibitor of the serotonin transporterPer Plenge0Ara M. Abramyan1Gunnar Sørensen2Arne Mørk3Pia Weikop4Ulrik Gether5Benny Bang-Andersen6Lei Shi7Claus J. Loland8Laboratory for Membrane Protein Dynamics. Department of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenComputational Chemistry and Molecular Biophysics Unit, Molecular Targets and Medications Discovery Branch, National Institute on Drug Abuse—Intramural Research Program, National Institutes of HealthLundbeck Research, H. Lundbeck A/SLundbeck Research, H. Lundbeck A/SLaboratory of Neuropsychiatry, Psychiatric Centre Copenhagen, University of CopenhagenDepartment of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenLundbeck Research, H. Lundbeck A/SComputational Chemistry and Molecular Biophysics Unit, Molecular Targets and Medications Discovery Branch, National Institute on Drug Abuse—Intramural Research Program, National Institutes of HealthLaboratory for Membrane Protein Dynamics. Department of Neuroscience, Faculty of Health and Medical Sciences, University of CopenhagenThe serotonin transporter (SERT) terminates serotonin signaling and its activity is modulated by antidepressants. Here authors reveal the mechanistic details underlying the coupling between the two binding sites in SERT and a high-affinity ligand for the allosteric site.https://doi.org/10.1038/s41467-020-15292-y
collection DOAJ
language English
format Article
sources DOAJ
author Per Plenge
Ara M. Abramyan
Gunnar Sørensen
Arne Mørk
Pia Weikop
Ulrik Gether
Benny Bang-Andersen
Lei Shi
Claus J. Loland
spellingShingle Per Plenge
Ara M. Abramyan
Gunnar Sørensen
Arne Mørk
Pia Weikop
Ulrik Gether
Benny Bang-Andersen
Lei Shi
Claus J. Loland
The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
Nature Communications
author_facet Per Plenge
Ara M. Abramyan
Gunnar Sørensen
Arne Mørk
Pia Weikop
Ulrik Gether
Benny Bang-Andersen
Lei Shi
Claus J. Loland
author_sort Per Plenge
title The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
title_short The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
title_full The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
title_fullStr The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
title_full_unstemmed The mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
title_sort mechanism of a high-affinity allosteric inhibitor of the serotonin transporter
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-03-01
description The serotonin transporter (SERT) terminates serotonin signaling and its activity is modulated by antidepressants. Here authors reveal the mechanistic details underlying the coupling between the two binding sites in SERT and a high-affinity ligand for the allosteric site.
url https://doi.org/10.1038/s41467-020-15292-y
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