To be, or not to be two sites: that is the question about LeuT substrate binding - Institut Pasteur Access content directly
Journal Articles Journal of General Physiology Year : 2011

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.
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pasteur-01655623 , version 1 (05-12-2017)

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Nicolas Reyes, Sotiria Tavoulari. To be, or not to be two sites: that is the question about LeuT substrate binding. Journal of General Physiology, 2011, 138 (4), pp.467 - 471. ⟨10.1085/jgp.201110652⟩. ⟨pasteur-01655623⟩

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