Ontology highlight
ABSTRACT:
SUBMITTER: Forrest LR
PROVIDER: S-EPMC1937540 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Forrest Lucy R LR Tavoulari Sotiria S Zhang Yuan-Wei YW Rudnick Gary G Honig Barry B
Proceedings of the National Academy of Sciences of the United States of America 20070724 31
The recent determination of the crystal structure of the leucine transporter from Aquifex aeolicus (aaLeuT) has provided significant insights into the function of neurotransmitter:sodium symporters. Transport by aaLeuT is Cl(-) independent, whereas many neurotransmitter:sodium symporters from higher organisms depend on Cl(-) ions. However, the only Cl(-) ion identified in the aaLeuT structure interacts with nonconserved residues in extracellular loops, and thus the relevance of this binding site ...[more]