Article
High-affinity cation binding to organic cation transporter 1 induces movement of helix 11 and blocks transport after mutations in a modeled interaction domain between two helices.
Molecular pharmacology - 1 Jan 2008
Gorbunov Dmitry, Gorboulev Valentin, Shatskaya Natalia, Mueller Thomas, Bamberg Ernst, Friedrich Thomas, Koepsell Hermann
Abstract excerpt
Voltage-clamp fluorometry was performed with a cysteine-deprived mutant of rat organic cation transporter 1 (rOCT1) in which Phe483 in transmembrane alpha-helix (TMH) 11 close to the extracellular surface was replaced by cysteine and labeled with tetramethylrhodamine-6-maleimide. Potential-dependent fluorescence changes were observed that were sensitive to presence of substrates choline, tetraethylammonium (TEA),...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
