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Mutational analysis of the high-affinity zinc binding site validates a refined human dopamine transp...

Mutational analysis of the high-affinity zinc binding site validates a refined human dopamine transp...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1314343754

Mutational analysis of the high-affinity zinc binding site validates a refined human dopamine transporter homology model

About this item

Full title

Mutational analysis of the high-affinity zinc binding site validates a refined human dopamine transporter homology model

Publisher

United States: Public Library of Science

Journal title

PLoS computational biology, 2013-02, Vol.9 (2), p.e1002909

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

The high-resolution crystal structure of the leucine transporter (LeuT) is frequently used as a template for homology models of the dopamine transporter (DAT). Although similar in structure, DAT differs considerably from LeuT in a number of ways: (i) when compared to LeuT, DAT has very long intracellular amino and carboxyl termini; (ii) LeuT and DA...

Alternative Titles

Full title

Mutational analysis of the high-affinity zinc binding site validates a refined human dopamine transporter homology model

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1314343754

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1314343754

Other Identifiers

ISSN

1553-7358,1553-734X

E-ISSN

1553-7358

DOI

10.1371/journal.pcbi.1002909

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