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Structural basis of organic cation transporter-3 inhibition
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Structural basis of organic cation transporter-3 inhibition
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Journal Article
Structural basis of organic cation transporter-3 inhibition
2022
Overview
Organic cation transporters (OCTs) facilitate the translocation of catecholamines, drugs and xenobiotics across the plasma membrane in various tissues throughout the human body. OCT3 plays a key role in low-affinity, high-capacity uptake of monoamines in most tissues including heart, brain and liver. Its deregulation plays a role in diseases. Despite its importance, the structural basis of OCT3 function and its inhibition has remained enigmatic. Here we describe the cryo-EM structure of human OCT3 at 3.2 Å resolution. Structures of OCT3 bound to two inhibitors, corticosterone and decynium-22, define the ligand binding pocket and reveal common features of major facilitator transporter inhibitors. In addition, we relate the functional characteristics of an extensive collection of previously uncharacterized human genetic variants to structural features, thereby providing a basis for understanding the impact of OCT3 polymorphisms.
The current work reports the structure of the human organic cation transporter 3 (OCT3 / SLC22A3) and provides the structural basis of its inhibition by two specific inhibitors, decynium-22 and corticosterone.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13
/ 13/1
/ 14
/ 14/33
/ 82/80
/ Cations
/ Corticosterone - pharmacology
/ Humanities and Social Sciences
/ Humans
/ Ligands
/ Lipids
/ Liver
/ Organic Cation Transport Proteins - genetics
/ Organic Cation Transport Proteins - metabolism
/ Organic Cation Transporter 1 - genetics
/ Organic Cation Transporter 1 - metabolism
/ Organic Cation Transporter 2 - metabolism
/ Science
