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Updated: May 29, 2026

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
To be, or not to be two sites: that is the question about LeuT substrate binding
Nicolas Reyes1, Sotiria Tavoulari
1Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA. sotiria.tavoulari@yale.edu
Abstract:
Transport proteins of the neurotransmitter sodium symporter (NSS) family regulate the extracellular concentration of several neurotransmitters in the central nervous system. The only member of this family for which atomic-resolution structural data are available is the prokaryotic homologue LeuT. This protein has been used as a model system to study the molecular mechanism of transport of the NSS family. In this Journal Club, we discuss two strikingly different LeuT transport mechanisms: one involving a single high-affinity substrate binding site and one recently proposed alternative involving two high-affinity substrate binding sites that are allosterically coupled.
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