The functional domains of dopamine transporter for cocaine analog, CFT binding
Experimental & Molecular Medicine
; : 90-94, 2002.
Article
em En
| WPRIM
| ID: wpr-228522
Biblioteca responsável:
WPRO
ABSTRACT
Cocaine analogue, CFT (2beta-carbomethoxy-3beta-(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 3rd and the 6-8th 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 3rd and 6-8th transmembrane domain (TM), and that these regions might contribute to form the 3-dimensional pocket for CFT binding.
Texto completo:
1
Base de dados:
WPRIM
Assunto principal:
Proteínas de Membrana Transportadoras
/
Ligação Proteica
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Proteínas Recombinantes de Fusão
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Estrutura Terciária de Proteína
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Cocaína
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Animais
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Experimental & Molecular Medicine
Ano de publicação:
2002
Tipo de documento:
Article