4L17
GluA2-L483Y-A665C ligand-binding domain in complex with the antagonist DNQX
Summary for 4L17
| Entry DOI | 10.2210/pdb4l17/pdb |
| Descriptor | Glutamate receptor 2, 6,7-DINITROQUINOXALINE-2,3-DIONE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | ion channel, neuroreceptor, membrane, transport protein |
| Biological source | Rattus norvegicus (brown rat,rat,rats) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: P19491 |
| Total number of polymer chains | 4 |
| Total formula weight | 118503.76 |
| Authors | Lau, A.Y.,Blachowicz, L.,Roux, B. (deposition date: 2013-06-02, release date: 2013-08-14, Last modification date: 2024-10-30) |
| Primary citation | Lau, A.Y.,Salazar, H.,Blachowicz, L.,Ghisi, V.,Plested, A.J.,Roux, B. A conformational intermediate in glutamate receptor activation. Neuron, 79:492-503, 2013 Cited by PubMed Abstract: Ionotropic glutamate receptors (iGluRs) transduce the chemical signal of neurotransmitter release into membrane depolarization at excitatory synapses in the brain. The opening of the transmembrane ion channel of these ligand-gated receptors is driven by conformational transitions that are induced by the association of glutamate molecules to the ligand-binding domains (LBDs). Here, we describe the crystal structure of a GluA2 LBD tetramer in a configuration that involves an ∼30° rotation of the LBD dimers relative to the crystal structure of the full-length receptor. The configuration is stabilized by an engineered disulfide crosslink. Biochemical and electrophysiological studies on full-length receptors incorporating either this crosslink or an engineered metal bridge show that this LBD configuration corresponds to an intermediate state of receptor activation. GluA2 activation therefore involves a combination of both intra-LBD (cleft closure) and inter-LBD dimer conformational transitions. Overall, these results provide a comprehensive structural characterization of an iGluR intermediate state. PubMed: 23931998DOI: 10.1016/j.neuron.2013.06.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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