Extended Data Fig. 5: The c-terminus of the hDATTwin:cocaine complex is fully resolved. | Nature

Extended Data Fig. 5: The c-terminus of the hDATTwin:cocaine complex is fully resolved.

From: Structure of the human dopamine transporter in complex with cocaine

Extended Data Fig. 5

a, EM density of the c-terminal domain of hDATTwin shown as black mesh with fitted structure as blue ribbon. Hydrophobic and hydrophilic residues of the amphipathic helix are shown as yellow and aqua sticks, respectively. Nitrogen, oxygen, and hydrogen atoms are shown in dark blue, red and white, respectively. b, The amphipathic c-terminal helix of hDATTwin:cocaine complex (blue) shown in colors representing hydrophobic (yellow) and hydrophilic (aqua) residues. The detergent micelle is shaded in gray with the outline marked with a solid black line. Below: a schematic representation of the helix demarcating the hydrophobic and hydrophilic sides with dashed lines in yellow and aqua, respectively.

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