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The sodium/substrate symporter family: structural and functional features
Author(s) -
Jung Heinrich
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03184-8
Subject(s) - symporter , sodium iodide symporter , chemistry , sodium , binding site , transmembrane protein , substrate (aquarium) , transmembrane domain , biochemistry , biophysics , stereochemistry , biology , amino acid , transporter , gene , receptor , ecology , organic chemistry
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.