Polyspecific Organic Cation Transport: Insights into the Substrate Binding Site
- Address correspondence to:
Gerhard Burckhardt, Abteilung Vegetative Physiologie und Pathophysiologie, Georg-August-Universität, Humboldtallee 23, 37073 Göttingen, Germany. E-mail: gburckh{at}gwdg.de
Abstract
Positively charged endogenous and exogenous organic compounds of diverse chemical structures are transported by polyspecific organic cation transporters (OCT). In two contributions to the May 2005 issue of Molecular Pharmacology, amino acid residues within the fourth and tenth transmembrane helices of rat OCT1 are described that contribute to cation and corticosterone binding. In a three-dimensional model based on the structure of the lactose permease, these residues are located in a large grove, the binding site for biogenic amines and cationic drugs.
Footnotes
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Article, publication date, and citation information can be found at http://molpharm.aspetjournals.org.
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doi:10.1124/mol.105.012161.
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Please see the related articles on pages page 1600 and page 1612.
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ABBREVIATIONS: OCT1, organic cation transporter 1; TEA, tetraethylammonium; MPP, 1-methyl-4-phenylpyridinium.
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- Received February 21, 2005.
- Accepted February 25, 2005.
- The American Society for Pharmacology and Experimental Therapeutics
