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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2002-03

AUTHORS

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

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. More... »

PAGES

90

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/emm.2002.13

DOI

http://dx.doi.org/10.1038/emm.2002.13

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014099577

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11989984


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