To be, or not to be two sites: that is the question about LeuT substrate binding - Archive ouverte HAL 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

(1) , (2)
1
2

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.
Fichier principal
Vignette du fichier
To be, or not to be two sites that is the question about LeuT substrate binding.pdf (1.21 Mo) Télécharger le fichier
Origin : Publication funded by an institution
Loading...

Dates and versions

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

Licence

Attribution - NonCommercial - ShareAlike - CC BY 4.0

Identifiers

Cite

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⟩

Collections

PASTEUR
104 View
64 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More