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Review
. 2002 Oct 2;529(1):73-7.
doi: 10.1016/s0014-5793(02)03184-8.

The Sodium/Substrate Symporter Family: Structural and Functional Features

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Free article
Review

The Sodium/Substrate Symporter Family: Structural and Functional Features

Heinrich Jung. FEBS Lett. .
Free article

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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