Abstract
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 Zn2+ ions. (S)-ATPA induces a domain closure of ca. 21° 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 (US) |
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Pages (from-to) | 872-875 |
Number of pages | 4 |
Journal | Journal of Medicinal Chemistry |
Volume | 46 |
Issue number | 5 |
DOIs | |
State | Published - Feb 27 2003 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Medicine
- Drug Discovery