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TitleCryo-EM structures of human OAT1 reveal drug binding and inhibition mechanisms.
Journal, issue, pagesStructure, Vol. 33, Issue 11, Page 1856-11866.e5, Year 2025
Publish dateNov 6, 2025
AuthorsHyung-Min Jeon / Jisung Eun / Kelly H Kim / Youngjin Kim /
PubMed AbstractThe organic anion transporter 1 (OAT1) plays a key role in excreting waste from organic drug metabolism and contributes significantly to drug-drug interactions and drug disposition. However, the ...The organic anion transporter 1 (OAT1) plays a key role in excreting waste from organic drug metabolism and contributes significantly to drug-drug interactions and drug disposition. However, the structural basis of specific substrate and inhibitor transport by human OAT1 (hOAT1) has remained elusive. We determined four cryogenic electron microscopy (cryo-EM) structures of hOAT1 in its inward-facing conformation: the apo form, the substrate (olmesartan)-bound form with different anions, and the inhibitor (probenecid)-bound form. Structural and functional analyses revealed that Ser203 has an auxiliary role in chloride coordination, and it is a critical residue modulating olmesartan transport via chloride ion interactions. Structural comparisons indicate that inhibitors not only compete with substrates, but also obstruct substrate exit and entry from the cytoplasmic side, thereby increasing inhibitor retention. The findings can support drug development by providing insights into substrate recognition and the mechanism by which inhibitors arrest the OAT1 transport cycle.
External linksStructure / PubMed:40845848
MethodsEM (single particle)
Resolution3.33 - 3.88 Å
Structure data

62390

9kkk

EMDB-62390, PDB-9kkk:
Cryo-EM structure of human SLC22A6 (OAT1) in the apo-state
Method: EM (single particle) / Resolution: 3.85 Å

62400

9kl5

EMDB-62400, PDB-9kl5:
Cryo-EM strucuture of human OAT1 in complex with probenecid
Method: EM (single particle) / Resolution: 3.33 Å

62418

9klz

EMDB-62418, PDB-9klz:
Human OAT1 in complex with olmesartan
Method: EM (single particle) / Resolution: 3.88 Å

64368

9unx

EMDB-64368, PDB-9unx:
Cryo-EM structure of human OAT1 in complex with olmesartan and bromide ion.
Method: EM (single particle) / Resolution: 3.45 Å

Chemicals

ChemComp-RTO:
4-(dipropylsulfamoyl)benzoic acid / medication*YM

ChemComp-CL:
Unknown entry

ChemComp-OLM:
Olmesartan / medication*YM

ChemComp-BR:
BROMIDE ION

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Antiporter / Organic Anion / drug-drug interaction. nephrotoxicity / membrane transporter / gout / drug-drug interaction / drug elimination / TRANSPORT PROTEIN / hypertension / kidney disease / transporter / substrate / organic anion.

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