To be, or not to be two sites: That is the question about LeuT substrate binding

17Citations
Citations of this article
54Readers
Mendeley users who have this article in their library.

This article is free to access.

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 atomicresolution 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. © 2011 Reyes and Tavoulari.

Cite

CITATION STYLE

APA

Reyes, N., & Tavoulari, S. (2011, October). To be, or not to be two sites: That is the question about LeuT substrate binding. Journal of General Physiology. https://doi.org/10.1085/jgp.201110652

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free