1NNK

X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.85 A resolution. Crystallization with zinc ions.

Summary for 1NNK

• Entry DOI: 10.2210/pdb1nnk/pdb
• Related: 1FTJ 1FTK 1FTL 1FTM 1FTO 1FW0 1GR2 1LB8 1LB9 1LBB 1LBC 1M5B 1M5C 1M5D 1M5E 1M5F 1MM6 1MM7 1MY3 1MY4 1NNP
• Descriptor: Glutamate receptor 2, ZINC ION, CHLORIDE ION, ... (5 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: 1
• Total formula weight: 29615.19

Authors

Lunn, M.-L.,Hogner, A.,Stensbol, T.B.,Gouaux, E.,Egebjerg, J.,Kastrup, J.S. (deposition date: 2003-01-14, release date: 2003-03-04, Last modification date: 2024-10-16)

Primary citation

Lunn, M.L.,Hogner, A.,Stensbol, T.B.,Gouaux, E.,Egebjerg, J.,Kastrup, J.S.
Three-Dimensional Structure of the Ligand-Binding Core of GluR2 in Complex with the Agonist (S)-ATPA: Implications for Receptor Subunit Selectivity.
J.Med.Chem., 46:872-875, 2003

PubMed 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 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.

PubMed: 12593667
DOI: 10.1021/jm021020+

Experimental method

X-RAY DIFFRACTION (1.85 Å)