Structure-Function of the High Affinity Substrate Binding Site (S1) of Human Norepinephrine Transporter.

docking guided mutagenesis molecular modeling monoamine transporter noradrenaline uptake structural determinants

Journal

Frontiers in pharmacology
ISSN: 1663-9812
Titre abrégé: Front Pharmacol
Pays: Switzerland
ID NLM: 101548923

Informations de publication

Date de publication:
2020
Historique:
received: 17 10 2019
accepted: 14 02 2020
entrez: 27 3 2020
pubmed: 27 3 2020
medline: 27 3 2020
Statut: epublish

Résumé

The human norepinephrine transporter (hNET) is a member of the neurotransmitter/sodium symporter family, which also includes the neuronal monoamine transporters for serotonin (SERT) and dopamine (DAT). Its involvement in chronic pain and many neurological disorders underlies its pharmaceutical importance. Using the X-ray crystal structures of the human serotonin transporter (hSERT) (PDB 5I6X) and

Identifiants

pubmed: 32210813
doi: 10.3389/fphar.2020.00217
pmc: PMC7066499
doi:

Types de publication

Journal Article

Langues

eng

Pagination

217

Informations de copyright

Copyright © 2020 Jha, Ragnarsson and Lewis.

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Auteurs

Prerna Jha (P)

Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.

Lotten Ragnarsson (L)

Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.

Richard J Lewis (RJ)

Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.

Classifications MeSH