| Autor: |
Lunn, M.-L., Hogner, A., Stensbol, T. B., Gouaux, E., Egebjerg, J., Kastrup, J. S. |
| Zdroj: |
Journal of Medicinal Chemistry; February 2003, Vol. 46 Issue: 5 p872-875, 4p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
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