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Dopamine reuptake and inhibitory mechanisms in human dopamine transporter.
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- Author(s): Li, Yue; Wang, Xianping; Meng, Yufei; Hu, Tuo; Zhao, Jun; Li, Renjie; Bai, Qinru; Yuan, Pu; Han, Jun; Hao, Kun; Wei, Yiqing; Qiu, Yunlong; Li, Na; Zhao, Yan
- Source:
Nature; Aug2024, Vol. 632 Issue 8025, p686-694, 9p - Source:
- Additional Information
- Abstract: The dopamine transporter has a crucial role in regulation of dopaminergic neurotransmission by uptake of dopamine into neurons and contributes to the abuse potential of psychomotor stimulants1–3. Despite decades of study, the structure, substrate binding, conformational transitions and drug-binding poses of human dopamine transporter remain unknown. Here we report structures of the human dopamine transporter in its apo state, and in complex with the substrate dopamine, the attention deficit hyperactivity disorder drug methylphenidate, and the dopamine-uptake inhibitors GBR12909 and benztropine. The dopamine-bound structure in the occluded state precisely illustrates the binding position of dopamine and associated ions. The structures bound to drugs are captured in outward-facing or inward-facing states, illuminating distinct binding modes and conformational transitions during substrate transport. Unlike the outward-facing state, which is stabilized by cocaine, GBR12909 and benztropine stabilize the dopamine transporter in the inward-facing state, revealing previously unseen drug-binding poses and providing insights into how they counteract the effects of cocaine. This study establishes a framework for understanding the functioning of the human dopamine transporter and developing therapeutic interventions for dopamine transporter-related disorders and cocaine addiction.Structural analyses of the human dopamine transporter in apo and substrate-bound states and in complex with drugs and inhibitors reveal key binding residues and conformational transitions that occur during substrate transport. [ABSTRACT FROM AUTHOR]
- Abstract: Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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