Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for prostaglandin and drug transport via SLCO2A1.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Mar 20, 2026
Authors	Chitra Joshi / Justin C Deme / Yoshinobu Nakamura / Wei-Tse Hsu / Jonathan D Goult / Takafumi Kato / Joanne L Parker / Philip C Biggin / Susan M Lea / Takeo Nakanishi / Simon Newstead /
PubMed Abstract	Organic anion-transporting polypeptide transporters (SLCO/OATPs) function as cellular gatekeepers, regulating intestinal absorption, hepatic and renal clearance, and the tissue distribution of drugs ...Organic anion-transporting polypeptide transporters (SLCO/OATPs) function as cellular gatekeepers, regulating intestinal absorption, hepatic and renal clearance, and the tissue distribution of drugs and metabolites in the human body. However, the mechanisms underlying substrate selection within the SLCO superfamily remain unclear, hampering efforts to rationalize the interaction of drugs and metabolites with these transporters. SLCO2A1 (also known as OATP2A1) is responsible for the distribution of eicosanoids, including prostaglandins (PGs) and thromboxanes, throughout the body, in addition to several families of nonsteroidal anti-inflammatory drugs (NSAIDs). Here, we present cryogenic electron microscopy structures of SLCO2A1 bound to endogenous PGs and to four widely prescribed medications for treating inflammation, chronic asthma, and Parkinson's disease (PD). Complementary molecular dynamics and in vivo cellular assays elucidate the molecular basis for PG and drug recognition. Our study reports essential mechanistic details that underpin substrate selection and subfamily adaptation within the broader SLCO superfamily of drug and metabolite transporters.
External links	Nat Commun / PubMed:41862483 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.4 Å
Structure data	53472 9qzo EMDB-53472, PDB-9qzo: Cryo-EM structure of rat SLCO2A1 in the apo state. Method: EM (single particle) / Resolution: 2.9 Å 53481 9r07 EMDB-53481, PDB-9r07: Cryo-EM structure of rat SLCO2A1 bound to zafirlukast. Method: EM (single particle) / Resolution: 3.2 Å 53482 9r0a EMDB-53482, PDB-9r0a: Cryo-EM structure of rat SLCO2A1 bound to fentiazac. Method: EM (single particle) / Resolution: 3.1 Å 53483 9r0i EMDB-53483, PDB-9r0i: Cryo-EM structure of rat SLCO2A1 bound to losartan. Method: EM (single particle) / Resolution: 3.1 Å 53484 9r0m EMDB-53484, PDB-9r0m: Cryo-EM structure of rat SLCO2A1 bound to prostaglandin E2. Method: EM (single particle) / Resolution: 3.2 Å 53485 9r0n EMDB-53485, PDB-9r0n: Cryo-EM structure of rat SLCO2A1 bound to dinoprost. Method: EM (single particle) / Resolution: 3.4 Å 53486 9r0o EMDB-53486, PDB-9r0o: Cryo-EM structure of rat SLCO2A1 bound to tolcapone. Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-Y01: CHOLESTEROL HEMISUCCINATE ChemComp-ZLK: zafirlukast / antagonistYM PDB-1jbl: Solution structure of SFTI-1, A cyclic trypsin inhibitor from sunflower seeds ChemComp-AV0: Lauryl Maltose Neopentyl Glycol ChemComp-LSN: [2-butyl-5-chloranyl-3-[[4-[2-(2H-1,2,3,4-tetrazol-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol / medicationYM ChemComp-P2E: (Z)-7-[(1R,2R,3R)-3-hydroxy-2-[(E,3S)-3-hydroxyoct-1-enyl]-5-oxo-cyclopentyl]hept-5-enoic acid / medicationYM ChemComp-UGU: (Z)-7-[(1R,2R,3R,5S)-3,5-bis(oxidanyl)-2-[(E,3S)-3-oxidanyloct-1-enyl]cyclopentyl]hept-5-enoic acid / hormoneYM ChemComp-TCW: Tolcapone / medication, inhibitor*YM
Source	rattus norvegicus (Norway rat)
Keywords	MEMBRANE PROTEIN / OATP2A1 / plasma membrane localized / prostaglandin transporter / PGT / major facilitator superfamily. / plasma membrane localised