DAT is composed of 12 transmembrane helices with intracellular N- and C-termini. The transporter has sites for sodium and chloride binding, essential for its function. The extracellular loops of DAT are glycosylated, which aids in proper folding and stability. High-resolution imaging techniques like cryo-electron microscopy have provided detailed structural insights into DAT, revealing how these transporters operate at a molecular level.
