Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters

Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters

The Drosophila dopamine transporter (dDAT) is a catecholamine neurotransmitter transporter that resembles the human norepinephrine transporter (hNET). Here the authors report X-ray structures of the dDAT in substrate-free form, norepinephrine-bound form and dDAT bound to commonly prescribed chronic...

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Main Authors: Shabareesh Pidathala, Aditya Kumar Mallela, Deepthi Joseph, Aravind Penmatsa
Format: Article
Language:English
Published: Nature Publishing Group 2021-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-22385-9
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spelling doaj-596e7b01288047a2ae7f7113ab49a0d62021-04-18T11:14:29ZengNature Publishing GroupNature Communications2041-17232021-04-0112111210.1038/s41467-021-22385-9Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transportersShabareesh Pidathala0Aditya Kumar Mallela1Deepthi Joseph2Aravind Penmatsa3Molecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of ScienceMolecular Biophysics Unit, Indian Institute of ScienceThe Drosophila dopamine transporter (dDAT) is a catecholamine neurotransmitter transporter that resembles the human norepinephrine transporter (hNET). Here the authors report X-ray structures of the dDAT in substrate-free form, norepinephrine-bound form and dDAT bound to commonly prescribed chronic pain inhibitors duloxetine, milnacipran and tramadol and shed light on the structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters.https://doi.org/10.1038/s41467-021-22385-9
collection DOAJ
language English
format Article
sources DOAJ
author Shabareesh Pidathala
Aditya Kumar Mallela
Deepthi Joseph
Aravind Penmatsa
spellingShingle Shabareesh Pidathala
Aditya Kumar Mallela
Deepthi Joseph
Aravind Penmatsa
Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
Nature Communications
author_facet Shabareesh Pidathala
Aditya Kumar Mallela
Deepthi Joseph
Aravind Penmatsa
author_sort Shabareesh Pidathala
title Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
title_short Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
title_full Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
title_fullStr Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
title_full_unstemmed Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
title_sort structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-04-01
description The Drosophila dopamine transporter (dDAT) is a catecholamine neurotransmitter transporter that resembles the human norepinephrine transporter (hNET). Here the authors report X-ray structures of the dDAT in substrate-free form, norepinephrine-bound form and dDAT bound to commonly prescribed chronic pain inhibitors duloxetine, milnacipran and tramadol and shed light on the structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters.
url https://doi.org/10.1038/s41467-021-22385-9
work_keys_str_mv AT shabareeshpidathala structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters
AT adityakumarmallela structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters
AT deepthijoseph structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters
AT aravindpenmatsa structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters
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