Abstract
X-ray structures of the GluR2 ligand-binding core in complex with (S)-Des-Me-AMPA and in the presence and absence of zinc ions have been determined. (S)-Des-Me-AMPA, which is devoid of a substituent in the 5-position of the isoxazolol ring, only has limited interactions with the partly hydrophobic pocket of the ligand-binding site, and adopts an AMPA-like binding mode. The structures, in comparison with other agonist complex structures, disclose the relative importance of the isoxazolol ring and of the substituent in the 5-position for the mode of binding. A relationship appears to exist between the extent of interaction of the ligand with the hydrophobic pocket and the affinity of the ligand.
Original language | English (US) |
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Pages (from-to) | 173-178 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 531 |
Issue number | 2 |
DOIs | |
State | Published - Nov 6 2002 |
Externally published | Yes |
Keywords
- AMPA analogue
- Agonist
- Ionotropic glutamate receptor
- Ligand-binding core
- X-ray crystallography
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology