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Updated: Jul 16, 2026
09:42
Deriving the Time Course of Glutamate Clearance with a Deconvolution Analysis of Astrocytic Transporter Currents
Published on: August 7, 2013
Gate movements in glutamate transporters
1Department of Biochemistry, Hebrew University, Hadassah Medical School, P.O. Box 12272, Jerusalem 91120, Israel. kannerb@cc.huji.ac.il
ACS Chemical Biology
|March 22, 2007
Summary
Sodium-coupled glutamate transporters facilitate brain communication by alternating binding sites. New structures reveal the outward-facing conformation, advancing understanding of these crucial ion-coupled transporters.
Area of Science:
- Neuroscience
- Structural Biology
- Biochemistry
Background:
- Sodium-coupled glutamate transporters are vital for synaptic plasticity and neuronal excitability.
- These transporters cycle between states, exposing binding sites to the synapse or intracellular space.
- Previous structural studies captured the substrate-occluded state of an archaeal homologue.
Purpose of the Study:
- To elucidate the structural basis of the outward-facing conformation in sodium-coupled glutamate transporters.
- To gain insights into the transport mechanism of these essential brain proteins.
Main Methods:
- X-ray crystallography was used to determine the structure of the archaeal homologue.
- The determined structure represents the outward-facing conformation of the transporter.
Main Results:
- The crystal structure of the archaeal glutamate transporter homologue in its outward-facing conformation was determined.
- This structure complements the previously solved substrate-occluded form.
Conclusions:
- The determined structures provide critical insights into the alternating access mechanism of sodium-coupled transporters.
- Understanding these structures aids in comprehending excitatory neurotransmission and potential therapeutic targets.
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