3DP6

Crystal structure of the binding domain of the AMPA subunit GluR2 bound to glutamate

Summary for 3DP6

• Entry DOI: 10.2210/pdb3dp6/pdb
• Related: 3DLN 3DP4
• Descriptor: Glutamate receptor 2, ZINC ION, GLUTAMIC ACID, ... (4 entities in total)
• Functional Keywords: glutamate receptor, glur2, ampa receptor, neurotransmitter receptor, s1s2, alternative splicing, cell junction, endoplasmic reticulum, glycoprotein, ion transport, ionic channel, lipoprotein, membrane, palmitate, phosphoprotein, postsynaptic cell membrane, rna editing, synapse, transmembrane, transport, signaling protein
• Biological source: Rattus norvegicus; More
• Cellular location: Cell membrane; Multi-pass membrane protein: P19491
• Total number of polymer chains: 3
• Total formula weight: 93265.16

Authors

Ahmed, A.H.,Wang, Q.,Sondermann, H.,Oswald, R.E. (deposition date: 2008-07-07, release date: 2008-11-25, Last modification date: 2024-10-30)

Primary citation

Ahmed, A.H.,Wang, Q.,Sondermann, H.,Oswald, R.E.
Structure of the S1S2 glutamate binding domain of GLuR3.
Proteins, 75:628-637, 2008

PubMed Abstract: Glutamate receptors are the most prevalent excitatory neurotransmitter receptors in the vertebrate central nervous system. Determining the structural differences between the binding sites of different subtypes is crucial to our understanding of neuronal circuits and to the development of subtype specific drugs. The structures of the binding domain (S1S2) of the GluR3 (flip) AMPA receptor subunit bound to glutamate and AMPA and the GluR2 (flop) subunit bound to glutamate were determined by X-ray crystallography to 1.9, 2.1, and 1.55 A, respectively. Overall, the structure of GluR3 (flip) S1S2 is very similar to GluR2 (flop) S1S2 (backbone RMSD of 0.30 +/- 0.05 for glutamate-bound and 0.26 +/- 0.01 for AMPA-bound). The differences in the flip and flop isoforms are subtle and largely arise from one hydrogen bond across the dimer interface and associated water molecules. Comparison of the binding affinity for various agonists and partial agonists suggest that the S1S2 domains of GluR2 and GluR3 show only small differences in affinity, unlike what is found for the intact receptors (with the exception of one ligand, Cl-HIBO, which has a 10-fold difference in affinity for GluR2 vs. GluR3).

PubMed: 19003990
DOI: 10.1002/prot.22274

Experimental method

X-RAY DIFFRACTION (1.55 Å)