The functional domains of dopamine transporter for cocaine analog, CFT binding

Sang-Hun Lee, Mi Yoon Chang, Dae Joon Jeon, Dong Yul Oh, Hyeon Son, Chang Ho Lee, Young Seek Lee, Yong Sung Lee

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Cocaine analogue, CFT (2β-carbomethoxy-3β-(4-fluorophenyl) tropane) binding to dopamine transporter (DAT) in different species is quite heterogeneous. CFT is scarcely detected in bovine DAT whereas it is conspicuous in humans. To examine the structural basis for this functional discrepancy, we analyzed transporter chimeras of these two DATs. The CFT binding activities are avid in all of the chimeric DATs of which both of the 3 rd and the 6-8 th transmembrane domain (TM) are composed of human DAT sequences. On the contrary, CFT binding activities were scarcely detected if either or both of two regions are replaced with bovine sequences. These findings indicate that the CFT binding absolutely requires human DAT sequences, at least, in the regions encompassing the 3 rd and 6-8 th transmembrane domain (TM), and that these regions might contribute to form the 3-dimensional pocket for CFT binding.

Original languageEnglish
Pages (from-to)90-94
Number of pages5
JournalExperimental and Molecular Medicine
Volume34
Issue number1
StatePublished - 2002 Mar 31

Fingerprint

Dopamine Plasma Membrane Transport Proteins
Cocaine

Keywords

  • CFT
  • CFT binding
  • Cocaine
  • Cocaine binding
  • Dopamine transporter (DAT)
  • Transmembrane domain

Cite this

Lee, Sang-Hun ; Chang, Mi Yoon ; Jeon, Dae Joon ; Oh, Dong Yul ; Son, Hyeon ; Lee, Chang Ho ; Lee, Young Seek ; Lee, Yong Sung. / The functional domains of dopamine transporter for cocaine analog, CFT binding. In: Experimental and Molecular Medicine. 2002 ; Vol. 34, No. 1. pp. 90-94.
@article{748189e5860e4f07bcd80a451b150dce,
title = "The functional domains of dopamine transporter for cocaine analog, CFT binding",
abstract = "Cocaine analogue, CFT (2β-carbomethoxy-3β-(4-fluorophenyl) tropane) binding to dopamine transporter (DAT) in different species is quite heterogeneous. CFT is scarcely detected in bovine DAT whereas it is conspicuous in humans. To examine the structural basis for this functional discrepancy, we analyzed transporter chimeras of these two DATs. The CFT binding activities are avid in all of the chimeric DATs of which both of the 3 rd and the 6-8 th transmembrane domain (TM) are composed of human DAT sequences. On the contrary, CFT binding activities were scarcely detected if either or both of two regions are replaced with bovine sequences. These findings indicate that the CFT binding absolutely requires human DAT sequences, at least, in the regions encompassing the 3 rd and 6-8 th transmembrane domain (TM), and that these regions might contribute to form the 3-dimensional pocket for CFT binding.",
keywords = "CFT, CFT binding, Cocaine, Cocaine binding, Dopamine transporter (DAT), Transmembrane domain",
author = "Sang-Hun Lee and Chang, {Mi Yoon} and Jeon, {Dae Joon} and Oh, {Dong Yul} and Hyeon Son and Lee, {Chang Ho} and Lee, {Young Seek} and Lee, {Yong Sung}",
year = "2002",
month = "3",
day = "31",
language = "English",
volume = "34",
pages = "90--94",
journal = "Experimental and Molecular Medicine",
issn = "1226-3613",
number = "1",

}

The functional domains of dopamine transporter for cocaine analog, CFT binding. / Lee, Sang-Hun; Chang, Mi Yoon; Jeon, Dae Joon; Oh, Dong Yul; Son, Hyeon; Lee, Chang Ho; Lee, Young Seek; Lee, Yong Sung.

In: Experimental and Molecular Medicine, Vol. 34, No. 1, 31.03.2002, p. 90-94.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The functional domains of dopamine transporter for cocaine analog, CFT binding

AU - Lee, Sang-Hun

AU - Chang, Mi Yoon

AU - Jeon, Dae Joon

AU - Oh, Dong Yul

AU - Son, Hyeon

AU - Lee, Chang Ho

AU - Lee, Young Seek

AU - Lee, Yong Sung

PY - 2002/3/31

Y1 - 2002/3/31

N2 - Cocaine analogue, CFT (2β-carbomethoxy-3β-(4-fluorophenyl) tropane) binding to dopamine transporter (DAT) in different species is quite heterogeneous. CFT is scarcely detected in bovine DAT whereas it is conspicuous in humans. To examine the structural basis for this functional discrepancy, we analyzed transporter chimeras of these two DATs. The CFT binding activities are avid in all of the chimeric DATs of which both of the 3 rd and the 6-8 th transmembrane domain (TM) are composed of human DAT sequences. On the contrary, CFT binding activities were scarcely detected if either or both of two regions are replaced with bovine sequences. These findings indicate that the CFT binding absolutely requires human DAT sequences, at least, in the regions encompassing the 3 rd and 6-8 th transmembrane domain (TM), and that these regions might contribute to form the 3-dimensional pocket for CFT binding.

AB - Cocaine analogue, CFT (2β-carbomethoxy-3β-(4-fluorophenyl) tropane) binding to dopamine transporter (DAT) in different species is quite heterogeneous. CFT is scarcely detected in bovine DAT whereas it is conspicuous in humans. To examine the structural basis for this functional discrepancy, we analyzed transporter chimeras of these two DATs. The CFT binding activities are avid in all of the chimeric DATs of which both of the 3 rd and the 6-8 th transmembrane domain (TM) are composed of human DAT sequences. On the contrary, CFT binding activities were scarcely detected if either or both of two regions are replaced with bovine sequences. These findings indicate that the CFT binding absolutely requires human DAT sequences, at least, in the regions encompassing the 3 rd and 6-8 th transmembrane domain (TM), and that these regions might contribute to form the 3-dimensional pocket for CFT binding.

KW - CFT

KW - CFT binding

KW - Cocaine

KW - Cocaine binding

KW - Dopamine transporter (DAT)

KW - Transmembrane domain

UR - http://www.scopus.com/inward/record.url?scp=0037204441&partnerID=8YFLogxK

M3 - Article

C2 - 11989984

AN - SCOPUS:0037204441

VL - 34

SP - 90

EP - 94

JO - Experimental and Molecular Medicine

JF - Experimental and Molecular Medicine

SN - 1226-3613

IS - 1

ER -