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Updated: Jun 12, 2025

Selection of Transporter-Targeted Inhibitory Nanobodies by Solid-Supported-Membrane SSM-Based Electrophysiology
Published on: May 3, 2021
In silico structural studies on the vesicular neutral amino acid transporter NTT4 (SLC6A17)
Jędrzej Kukułowicz1, Marek Bajda1
1Department of Physicochemical Drug Analysis, Faculty of Pharmacy, Jagiellonian University Medical College, Medyczna 9, Krakow 30-688, Poland.
Abstract:
NTT4 is one of the neutral amino acid transporters that regulate neural concentration of precursors for glutamate biosynthesis. Here, we provide insight into the structure of NTT4 and rationalize substrate selectivity. Furthermore, we demonstrate how the mutations associated with mental disabilities imply malfunction of the transporter at the molecular level. We also compared the structures of NTT4 and B0AT2 (SLC6A15), which is a close homolog, sharing 66 % of the common amino acids. Our analyses may be useful in the search for compounds that inhibit substrate transport. Moreover, they allow a better understanding of the function of these transporters.
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