1MS7

X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.97 A resolution, Crystallization in the presence of zinc acetate

Summary for 1MS7

• Entry DOI: 10.2210/pdb1ms7/pdb
• Related: 1FTJ 1FTK 1FTL 1FTM 1FTO 1FWO 1GR2 1LB8 1LB9 1LBB 1LBC 1M5B 1M5C 1M5D 1M5E 1M5F 1MM6 1MM7
• Descriptor: Glutamate receptor subunit 2, ZINC ION, (S)-2-AMINO-3-(3-HYDROXY-ISOXAZOL-4-YL)PROPIONIC ACID, ... (4 entities in total)
• Functional Keywords: ionotropic glutamate receptor glur2, ligand-binding core, agonist complex, membrane protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P19491
• Total number of polymer chains: 3
• Total formula weight: 88573.92

Authors

Kasper, C.,Lunn, M.-L.,Liljefors, T.,Gouaux, E.,Egebjerg, J.,Kastrup, J.S. (deposition date: 2002-09-19, release date: 2003-07-08, Last modification date: 2024-11-06)

Primary citation

Kasper, C.,Lunn, M.-L.,Liljefors, T.,Gouaux, E.,Egebjerg, J.,Kastrup, J.S.
GluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists
FEBS Lett., 531:173-178, 2002

PubMed 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.

PubMed: 12417307
DOI: 10.1016/S0014-5793(02)03496-8

Experimental method

X-RAY DIFFRACTION (1.97 Å)