9NR7
The structure of GluA1/A4 LBD-TMD in Noelin-AMPAR complex
Summary for 9NR7
| Entry DOI | 10.2210/pdb9nr7/pdb |
| EMDB information | 49724 |
| Descriptor | Glutamate receptor 1, Isoform 2 of Glutamate receptor 4, Auxiliary protein at A'/C', ... (5 entities in total) |
| Functional Keywords | iglur, cp-ampa receptors, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 8 |
| Total formula weight | 256873.95 |
| Authors | Fang, C.L.,Gouaux, E. (deposition date: 2025-03-14, release date: 2025-07-02, Last modification date: 2025-11-26) |
| Primary citation | Fang, C.L.,Spangler, C.J.,Park, J.,Sheldon, N.,Trussell, L.O.,Gouaux, E. Gating and noelin clustering of native Ca 2+ -permeable AMPA receptors. Nature, 645:526-534, 2025 Cited by PubMed Abstract: AMPA-type ionotropic glutamate receptors (AMPARs) are integral to fast excitatory synaptic transmission and play vital roles in synaptic plasticity, motor coordination, learning, and memory. While extensive structural studies have been conducted on recombinant AMPARs and native calcium impermeable (CI)-AMPARs alongside their auxiliary proteins, the molecular architecture of native calcium permeable (CP)-AMPARs has remained undefined. To elucidate the subunit composition, physiological architecture, and gating mechanisms of CP-AMPARs, here we present the first visualization of these receptors, immunoaffinity purified from rat cerebella, and resolve their structures using cryo-electron microscopy (cryo-EM). Our results indicate that the predominant assembly consists of GluA1 and GluA4 subunits, with the GluA4 subunit occupying the B and D positions, while auxiliary subunits, including TARPs, are located at the B'/D' positions and CNIHs or TARPs at the A'/C' positions. Furthermore, we resolved the structure of the Noelin 1-GluA1/A4 complex, wherein Noelin 1 (Noe 1) specifically binds to the GluA4 subunit at the B and D positions. Notably, Noe 1 stabilizes the amino-terminal domain (ATD) layer without affecting receptor gating properties. Noe 1 contributes to AMPAR function by forming dimeric-AMPAR assemblies that likely engage in extracellular networks, clustering receptors within synaptic environments and modulating receptor responsiveness to synaptic inputs. PubMed: 40550474DOI: 10.1038/s41586-025-09289-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.18 Å) |
Structure validation
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