title: To be, or not to be two sites: that is the question about LeuT substrate binding.
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.
authors.affiliation: Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA. sotiria.tavoulari@yale.edu
authors.forename: Nicolas
authors.initials: N
authors.lastname: Reyes
authors.forename: Sotiria
authors.initials: S
authors.lastname: Tavoulari
mesh_terms: D001665:Binding Sites; D005786:Gene Expression Regulation; D006801:Humans; D008958:Models, Molecular; D050480:Plasma Membrane Neurotransmitter Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D050480:Plasma Membrane Neurotransmitter Transport Proteins