Journal
JOURNAL OF GENERAL PHYSIOLOGY
Volume 138, Issue 4, Pages 467-471Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.201110652
Keywords
-
Categories
Ask authors/readers for more resources
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
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available