3B7D
Crystal structure of the GLUR2 ligand binding core (HS1S2J) in complex with CNQX at 2.5 A resolution
Summary for 3B7D
| Entry DOI | 10.2210/pdb3b7d/pdb |
| Related | 1FTJ 1FTL 1FTM 1FTO |
| Descriptor | Glutamate receptor 2, 7-nitro-2,3-dioxo-2,3-dihydroquinoxaline-6-carbonitrile (3 entities in total) |
| Functional Keywords | s1s2, cnqx, structural genomics, psi-2, protein structure initiative, center for structures of membrane proteins, csmp, cell junction, glycoprotein, ion transport, ionic channel, lipoprotein, palmitate, phosphorylation, postsynaptic cell membrane, receptor, rna editing, synapse, transmembrane, transport, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: P19491 |
| Total number of polymer chains | 8 |
| Total formula weight | 234461.52 |
| Authors | Hays, F.A.,Center for Structures of Membrane Proteins (CSMP) (deposition date: 2007-10-30, release date: 2007-11-20, Last modification date: 2024-11-20) |
| Primary citation | Menuz, K.,Stroud, R.M.,Nicoll, R.A.,Hays, F.A. TARP auxiliary subunits switch AMPA receptor antagonists into partial agonists. Science, 318:815-817, 2007 Cited by PubMed Abstract: Quinoxalinedione compounds such as 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) are the most commonly used alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor antagonists. However, we find that in the presence of transmembrane AMPA receptor regulatory proteins (TARPs), which are AMPA receptor auxiliary subunits, CNQX acts as a partial agonist. CNQX induced small depolarizing currents in neurons of the central nervous system, and reconstitution of this agonist activity required coexpression of TARPs. A crystal structure of CNQX bound to the TARP-less AMPA receptor ligand-binding domain showed that, although CNQX induces partial domain closure, this movement is not transduced into linker separation, suggesting that TARPs may increase agonist efficacy by strengthening the coupling between domain closure and channel opening. Our results demonstrate that the presence of an auxiliary subunit can determine whether a compound functions as an agonist or antagonist. PubMed: 17975069DOI: 10.1126/science.1146317 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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