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Dimerization and antidepressant recognition at noradrenaline transporter
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Dimerization and antidepressant recognition at noradrenaline transporter
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Journal Article
Dimerization and antidepressant recognition at noradrenaline transporter
2024
Overview
The noradrenaline transporter has a pivotal role in regulating neurotransmitter balance and is crucial for normal physiology and neurobiology
1
. Dysfunction of noradrenaline transporter has been implicated in numerous neuropsychiatric diseases, including depression and attention deficit hyperactivity disorder
2
. Here we report cryo-electron microscopy structures of noradrenaline transporter in apo and substrate-bound forms, and as complexes with six antidepressants. The structures reveal a noradrenaline transporter dimer interface that is mediated predominantly by cholesterol and lipid molecules. The substrate noradrenaline binds deep in the central binding pocket, and its amine group interacts with a conserved aspartate residue. Our structures also provide insight into antidepressant recognition and monoamine transporter selectivity. Together, these findings advance our understanding of noradrenaline transporter regulation and inhibition, and provide templates for designing improved antidepressants to treat neuropsychiatric disorders.
Cryo-electron microscopy structures of the noradrenaline transporter in the apo state, bound to noradrenaline and bound to various antidepressants shed light on the substrate transport, molecular recognition and dimeric architecture of this protein.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/16
/ 82/29
/ 82/83
/ 96/109
/ Antidepressive Agents - chemistry
/ Antidepressive Agents - metabolism
/ Antidepressive Agents - pharmacology
/ Apoproteins - ultrastructure
/ Attention deficit hyperactivity disorder
/ Dopamine
/ Humanities and Social Sciences
/ Humans
/ Kinases
/ Lipids
/ Norepinephrine Plasma Membrane Transport Proteins - antagonists & inhibitors
/ Norepinephrine Plasma Membrane Transport Proteins - chemistry
/ Norepinephrine Plasma Membrane Transport Proteins - metabolism
/ Norepinephrine Plasma Membrane Transport Proteins - ultrastructure
/ Science
