Cytoplasmic pathway of SERT and repeat structure of LeuTA: Cytoplasmic pathway of serotonin transporter SERT is lined by amino acid residues (spheres)

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Presentation transcript:

Cytoplasmic pathway of SERT and repeat structure of LeuTA: Cytoplasmic pathway of serotonin transporter SERT is lined by amino acid residues (spheres) from transmembrane helices 1 (red), 5 (pale green), 6 (green), and 8 (cyan). Cytoplasmic pathway of SERT and repeat structure of LeuTA: Cytoplasmic pathway of serotonin transporter SERT is lined by amino acid residues (spheres) from transmembrane helices 1 (red), 5 (pale green), 6 (green), and 8 (cyan). The model of SERT was built by homology to LeuT and is viewed from the plane of the membrane with the backbone trace in ribbons, with bound serotonin (yellow), chloride (magenta), and sodium ions (dark blue) shown as spheres. B–D: the LeuT fold contains inverted topology repeats of five trans-membrane helices. Repeat A contains transmembrane helices 1–5 (B), and repeat B consists of transmembrane helices 6–10 (C), according to the LeuT numbering. Superposition (D) of the last three transmembrane helices from each of those repeats (pale colors) indicates a relative difference in the orientation of the first two transmembrane helices (dark colors). These two conformations of the repeats may contain the essence of the two alternating-access states of the transporter. Lucy R. Forrest, and Gary Rudnick Physiology 2009;24:377-386 ©2009 by American Physiological Society