Exploring the Structural Dynamics of LeuT Using EPR Spectroscopy: A Focus on Transmembrane Helix 10.

ABSTRACT: The amino-acid transporter LeuT from Aquifex aeolicus is a well-studied bacterial homologue of the neurotransmitter: sodium symporters (NSS), especially the solute carrier 6 (SLC6) family. Within the nervous system, SLC6 transporters play a vital role in the termination of synaptic transmission, and their dysfunction leads to severe neurological conditions, rendering them key pharmacological targets. LeuT was the first SLC6 homologue to be crystallised and remains the main reference transporter to develop transport cycle models for its eukaryotic counterparts. Here, we aim to probe LeuT and investigate mechanistically important conformational changes using a combination of Site-Directed Spin Labelling (SDSL) and Electron Paramagnetic Resonance (EPR) spectroscopic techniques in detergent so

SUBMITTER: Tsalagradas P 

PROVIDER: S-EPMC11886772 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature