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.
Type de document :
Article dans une revue
Journal of General Physiology, Rockefeller University Press, 2011, 138 (4), pp.467 - 471. 〈10.1085/jgp.201110652〉
https://hal-pasteur.archives-ouvertes.fr/pasteur-01655623
Contributeur : Nicolas Reyes
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Soumis le : mardi 5 décembre 2017 - 09:51:16
Dernière modification le : lundi 26 février 2018 - 16:26:01
Nicolas Reyes, Sotiria Tavoulari. To be, or not to be two sites: that is the question about LeuT substrate binding. Journal of General Physiology, Rockefeller University Press, 2011, 138 (4), pp.467 - 471. 〈10.1085/jgp.201110652〉. 〈pasteur-01655623〉
