Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity
Research output: Contribution to journal › Journal article › Research › peer-review
Marie-Louise Lunn, Anders Hogner, Tine B Stensbøl, Eric Gouaux, Jan Egebjerg, Jette Sandholm Jensen Kastrup
Two X-ray structures of the GluR2 ligand-binding core in complex with (S)-2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionic acid ((S)-ATPA) have been determined with and without Zn(2+) ions. (S)-ATPA induces a domain closure of ca. 21 degrees compared to the apo form. The tert-butyl moiety of (S)-ATPA is buried in a partially hydrophobic pocket and forces the ligand into the glutamate-like binding mode. The structures provide new insight into the molecular basis of agonist selectivity between AMPA and kainate receptors.
|Journal||Journal of Medicinal Chemistry|
|Number of pages||4|
|Publication status||Published - 27 Feb 2003|
- Binding Sites, Crystallography, X-Ray, Dimerization, Excitatory Amino Acid Agonists, Isoxazoles, Ligands, Models, Molecular, Propionates, Protein Conformation, Protein Subunits, Receptors, AMPA, Stereoisomerism, Zinc