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Towards an understanding of organic anion transporters: Structure–function relationships
Author(s) -
You Guofeng
Publication year - 2004
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/med.20014
Subject(s) - transporter , transmembrane protein , organic anion transporter 1 , transmembrane domain , solute carrier family , extracellular , drug , function (biology) , intracellular , biochemistry , organic anion , amino acid , biology , organic cation transport proteins , chemistry , membrane transport , pharmacology , computational biology , microbiology and biotechnology , receptor , membrane , gene , ion , organic chemistry
Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including anti‐viral drugs, anti‐tumor drugs, antibiotics, anti‐hypertensives, and anti‐inflammatories. The activities of OATs are directly linked to drug toxicity and drug–drug interactions. So far, four members of the OAT family have been identified: OAT1, OAT2, OAT3, and OAT4. These transporters share several common structural features including 12 transmembrane domains, multiple glycosylation sites localized in the first extracellular loop between transmembrane domains 1 and 2, and multiple phosphorylation sites present in the intracellular loop between transmembrane domains 6 and 7, and in the carboxyl terminus. The impact of these structural features on the function of these transporters has just begun to be explored. In the present review, the author will summarize recent progress made from her laboratory as well as from others, on the molecular characterization of the structure–function relationships of OATs, including particular amino acid residues/regions of the transporter protein (“molecular domains”) that potentially determine transport characteristics. © 2004 Wiley Periodicals, Inc. Med Res Rev, 24, No. 6, 762–774, 2004