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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Autores principales:	Shabareesh Pidathala, Aditya Kumar Mallela, Deepthi Joseph, Aravind Penmatsa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/596e7b01288047a2ae7f7113ab49a0d6
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spelling	oai:doaj.org-article:596e7b01288047a2ae7f7113ab49a0d62021-12-02T15:51:07ZStructural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters10.1038/s41467-021-22385-92041-1723https://doaj.org/article/596e7b01288047a2ae7f7113ab49a0d62021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22385-9https://doaj.org/toc/2041-1723The 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.Shabareesh PidathalaAditya Kumar MallelaDeepthi JosephAravind PenmatsaNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Shabareesh Pidathala Aditya Kumar Mallela Deepthi Joseph Aravind Penmatsa Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters
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.
format	article
author	Shabareesh Pidathala Aditya Kumar Mallela Deepthi Joseph Aravind Penmatsa
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 Portfolio
publishDate	2021
url	https://doaj.org/article/596e7b01288047a2ae7f7113ab49a0d6
work_keys_str_mv	AT shabareeshpidathala structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters AT adityakumarmallela structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters AT deepthijoseph structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters AT aravindpenmatsa structuralbasisofnorepinephrinerecognitionandtransportinhibitioninneurotransmittertransporters
_version_	1718385633442922496

Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters

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