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	Cryo-EM structures of human organic anion transporting polypeptide OATP1B1.
Journal, issue, pages	Cell Res, Vol. 33, Issue 12, Page 940-951, Year 2023
Publish date	Sep 6, 2023
Authors	Ziyang Shan / Xuemei Yang / Huihui Liu / Yafei Yuan / Yuan Xiao / Jing Nan / Wei Zhang / Wenqi Song / Jufang Wang / Feiwen Wei / Yanqing Zhang /
PubMed Abstract	Members of the solute carrier organic anion transporting polypeptide (OATPs) family function as transporters for a large variety of amphipathic organic anions including endogenous metabolites and ...Members of the solute carrier organic anion transporting polypeptide (OATPs) family function as transporters for a large variety of amphipathic organic anions including endogenous metabolites and clinical drugs, such as bile salts, steroids, thyroid hormones, statins, antibiotics, antivirals, and anticancer drugs. OATP1B1 plays a vital role in transporting such substances into the liver for hepatic clearance. FDA and EMA recommend conducting in vitro testing of drug-drug interactions (DDIs) involving OATP1B1. However, the structure and working mechanism of OATPs still remains elusive. In this study, we determined cryo-EM structures of human OATP1B1 bound with representative endogenous metabolites (bilirubin and estrone-3-sulfate), a clinical drug (simeprevir), and a fluorescent indicator (2',7'-dichlorofluorescein), in both outward- and inward-open states. These structures reveal major and minor substrate binding pockets and conformational changes during transport. In combination with mutagenesis studies and molecular dynamics simulations, our work comprehensively elucidates the transport mechanism of OATP1B1 and provides the structural basis for DDI predictions involving OATP1B1, which will greatly promote our understanding of OATPs.
External links	Cell Res / PubMed:37674011 / PubMed Central
Methods	EM (single particle)
Resolution	2.92 - 3.73 Å
Structure data	34909 8hnb EMDB-34909, PDB-8hnb: Cryo-EM structure of human OATP1B1 in apo state Method: EM (single particle) / Resolution: 3.53 Å 34910 8hnc EMDB-34910, PDB-8hnc: Cryo-EM structure of human OATP1B1 in complex with bilirubin Method: EM (single particle) / Resolution: 3.73 Å 34911 8hnd EMDB-34911, PDB-8hnd: Cryo-EM structure of human OATP1B1 in complex with estrone-3-sulfate Method: EM (single particle) / Resolution: 3.19 Å 34913 8hnh EMDB-34913, PDB-8hnh: Cryo-EM structure of human OATP1B1 in complex with simeprevir Method: EM (single particle) / Resolution: 3.73 Å 36922 8k6l EMDB-36922, PDB-8k6l: Cryo-EM structure of human OATP1B1 in complex with DCF Method: EM (single particle) / Resolution: 2.92 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine ChemComp-BLR: 3-[5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(Z)-(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoic acid / Bilirubin ChemComp-FY5: estrone 3-sulfate / medication, hormoneYM / Estrone sulfate ChemComp-30B: (2R,3aR,10Z,11aS,12aR,14aR)-N-(cyclopropylsulfonyl)-2-({7-methoxy-8-methyl-2-[4-(1-methylethyl)-1,3-thiazol-2-yl]quinolin-4-yl}oxy)-5-methyl-4,14-dioxo-2,3,3a,4,5,6,7,8,9,11a,12,13,14,14a-tetradecahydrocyclopenta[c]cyclopropa[g][1,6]diazacyclotetradecine-12a(1H)-carboxamide / medicationYM / Simeprevir ChemComp-IOQ: 2',7'-bis(chloranyl)-3',6'-bis(oxidanyl)spiro[2-benzofuran-3,9'-xanthene]-1-one
Source	homo sapiens (human)
Keywords	MEMBRANE PROTEIN / transporter / OATP1B1 / organic anion transporting peptide