ArticleNature communications2025
Structural basis of drug recognition by human MATE1 transporter.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Population pharmacokinetic modeling of amisulpride drug interactions and a transporter binding analysis.European journal of clinical pharmacology · 2026Article
- Characterization of blood-brain barrier L-arginine uptake using in situ brain perfusions in a female mouse model.Fluids and barriers of the CNS · 2026Article
- Identification of Brimonidine as a Novel Substrate of Organic Cation Transporters OCT2 and MATE1 Expressed in Human Eye.Investigative ophthalmology & visual science · 2026Article
- New Multicomponent Crystals of Antidiabetic Drug, Metformin: Mechanochemistry, Structural Studies, Biological Activity and Topological Analysis.International journal of molecular sciences · 2026Article
- Short-Chain and Long-Chain Fatty Acid-Containing Platinum-Acridine Anticancer Prodrugs: Exploiting Alternative Mechanisms of Cellular Internalization.Journal of medicinal chemistry · 2026Article
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Authors and funding
9 authors.
Funding
Abstract
Human MATE1 (multidrug and toxin extrusion protein 1) is highly expressed in the kidney and liver, where it mediates the final step in the excretion of a broad range of cationic drugs, including the antidiabetic drug metformin, into the urine and bile. This transport process is essential for drug clearance and also affects therapeutic efficacy. To understand the molecular basis of drug recognition by hMATE1, we determined cryo-electron microscopy structures of the transporter in complex with the substrates 1-methyl-4-phenylpyridinium (MPP) and metformin and with the inhibitor cimetidine. The structures reveal a shared binding site located in a negatively charged pocket in the C-lobe of the protein. We functionally validated key interactions using radioactivity-based cellular uptake assays using hMATE1 mutants. Molecular dynamics simulations provide insights into the different binding modes and dynamic behaviour of the ligands within the pocket. Collectively, these findings define the structural basis of hMATE1 substrate specificity and shed light on its role in drug transport and drug-drug interactions.
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