3DLN
Crystal structure of the binding domain of the AMPA subunit GluR3 bound to glutamate
Summary for 3DLN
| Entry DOI | 10.2210/pdb3dln/pdb |
| Descriptor | Glutamate receptor 3, ZINC ION, GLUTAMIC ACID, ... (4 entities in total) |
| Functional Keywords | glutamate receptor, glur3, ampa receptor, neurotransmitter receptor, s1s2, alternative splicing, cell junction, glycoprotein, ion transport, ionic channel, lipoprotein, membrane, palmitate, phosphoprotein, postsynaptic cell membrane, synapse, transmembrane, transport, signaling protein |
| Biological source | Rattus norvegicus More |
| Cellular location | Cell membrane ; Multi-pass membrane protein : P19492 |
| Total number of polymer chains | 1 |
| Total formula weight | 31099.07 |
| Authors | Ahmed, A.H.,Wang, Q.,Sondermann, H.,Oswald, R.E. (deposition date: 2008-06-27, 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 Cited by 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: 19003990DOI: 10.1002/prot.22274 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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