Evidence for distinct sodium-, dopamine-, and cocaine-dependent conformational changes in transmembrane segments 7 and 8 of the dopamine transporter
Previously we obtained evidence based on engineering of Zn 2+ binding sites that the
extracellular parts of transmembrane segment 7 (TM7) and TM8 in the human dopamine
transporter are important for transporter function. To further evaluate the role of this domain,
we have employed the substituted cysteine accessibility method and performed 10 single
cysteine substitutions at the extracellular ends of TM7 and TM8. The mutants were made in
background mutants of the human dopamine transporter with either two (E2C) or five …
extracellular parts of transmembrane segment 7 (TM7) and TM8 in the human dopamine
transporter are important for transporter function. To further evaluate the role of this domain,
we have employed the substituted cysteine accessibility method and performed 10 single
cysteine substitutions at the extracellular ends of TM7 and TM8. The mutants were made in
background mutants of the human dopamine transporter with either two (E2C) or five …
