Accessibility and Conformational Coupling in Serotonin Transporter Predicted Internal Domains

@article{AndroutsellisTheotokis2002AccessibilityAC,
  title={Accessibility and Conformational Coupling in Serotonin Transporter Predicted Internal Domains},
  author={Andreas Androutsellis-Theotokis and Gary Rudnick},
  journal={The Journal of Neuroscience},
  year={2002},
  volume={22},
  pages={8370 - 8378}
}
The intracellular topology of serotonin transporter (SERT) was examined using mutants containing single cysteine residues in the predicted cytoplasmic domain of the protein. Cysteine residues in each predicted cytoplasmic domain, including the NH2 and COOH termini and the five predicted internal loops, reacted with methanethiosulfonate (MTS) reagents only when the plasma membrane was permeabilized with digitonin or in membrane preparations but not in intact cells. The reaction was monitored by… 

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