The sodium/substrate symporter family: structural and functional features
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Updated: Sep 29, 2026

Selection of Transporter-Targeted Inhibitory Nanobodies by Solid-Supported-Membrane (SSM)-Based Electrophysiology
Published on: May 3, 2021
1Universität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, D-49069, Osnabrück, Germany. jung_h@biologie.uni-osnabrueck.de
Abstract:
Members of the sodium/substrate symporter family (SSSF, TC 2.A.21) catalyze the uptake of a wide variety of solutes including sugars, proline, pantothenate, and iodide into cells of pro- and eukaryotic origin. Extensive analyses of the topology of different SSSF proteins suggest an arrangement of 13 transmembrane domains as a common topological motif. Regions involved in sodium and/or substrate binding were identified. Furthermore, protein chemical and spectroscopic studies reveal ligand-induced structural alterations which are consistent with close interactions between the sites of sodium and substrate binding, thereby supporting an ordered binding mechanism for transport.
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