Monitoring conformational changes in the human neurotransmitter transporter homologue LeuT with ¹⁹F-NMR spectroscopy.

ABSTRACT: Neurotransmitter:sodium symporters (NSS) reuptake neurotransmitter molecules from the synaptic space through Na⁺-coupled transport. They are thought to work via the alternating access mechanism, exploring multiple configurations dictated by the binding of substrates and ions. Much of the current knowledge about these transporters has been derived from examining the structure of the Leucine Transporter (LeuT), a bacterial counterpart to human NSSs. Multiple crystal structures of LeuT provided valuable information regarding the steps involved in this mechanism. Dynamical data connecting the crystal structure to the transport cycle are critical to understanding how ligands are translated through the membrane. In the present study, we applied ¹⁹F-based nuclear magnetic re

SUBMITTER: Daminato A 

PROVIDER: S-EPMC11649037 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature