Article
Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions.
Proceedings of the National Academy of Sciences of the United States of America - 28 Jul 2009
Chaudhry Charu, Plested Andrew J R, Schuck Peter, Mayer Mark L
Abstract excerpt
The activity of many ligand-gated ion channels and cell surface receptors is modulated by small molecules and ions, but an understanding of the underlying molecular mechanisms is scarce. For kainate, but not AMPA subtype glutamate receptors, the binding of Na(+) and Cl(-) ions to discrete, electrostatically coupled sites in the extracellular ligand binding domain (LBD) dimer assembly regulates the rate of entry...
Topics
- Allosteric Regulation
- Amino Acid Sequence
- Binding Sites
- Calcium
- Cell Line
- Chlorides
- Energy Transfer
- Kinetics
- Ligands
- Models, Molecular
- Molecular Sequence Data