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
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.
Original language | English |
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Journal | Journal of Medicinal Chemistry |
Volume | 46 |
Issue number | 5 |
Pages (from-to) | 872-5 |
Number of pages | 4 |
ISSN | 0022-2623 |
DOIs | |
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
Research areas
ID: 44729638