3J6J
3.6 Angstrom resolution MAVS filament generated from helical reconstruction
Summary for 3J6J
| Entry DOI | 10.2210/pdb3j6j/pdb |
| EMDB information | 5922 5925 |
| Descriptor | Mitochondrial antiviral-signaling protein (1 entity in total) |
| Functional Keywords | card, mavs, innate immunity, rig-i, mda5, spontaneous filament formation, seeded filament formation, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 8 |
| Total formula weight | 90414.56 |
| Authors | Wu, B.,Peisley, A.,Li, Z.,Egelman, E.,Walz, T.,Penczek, P.,Hur, S. (deposition date: 2014-03-13, release date: 2014-07-30, Last modification date: 2024-02-21) |
| Primary citation | Wu, B.,Peisley, A.,Tetrault, D.,Li, Z.,Egelman, E.H.,Magor, K.E.,Walz, T.,Penczek, P.A.,Hur, S. Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I. Mol.Cell, 55:511-523, 2014 Cited by PubMed Abstract: RIG-I activates interferon signaling pathways by promoting filament formation of the adaptor molecule, MAVS. Assembly of the MAVS filament is mediated by its CARD domain (CARD(MAVS)), and requires its interaction with the tandem CARDs of RIG-I (2CARD(RIG-I)). However, the precise nature of the interaction between 2CARD(RIG-I) and CARD(MAVS), and how this interaction leads to CARD(MAVS) filament assembly, has been unclear. Here we report a 3.6 Å electron microscopy structure of the CARD(MAVS) filament and a 3.4 Å crystal structure of the 2CARD(RIG-I):CARD(MAVS) complex, representing 2CARD(RIG-I) "caught in the act" of nucleating the CARD(MAVS) filament. These structures, together with functional analyses, show that 2CARD(RIG-I) acts as a template for the CARD(MAVS) filament assembly, by forming a helical tetrameric structure and recruiting CARD(MAVS) along its helical trajectory. Our work thus reveals that signal activation by RIG-I occurs by imprinting its helical assembly architecture on MAVS, a previously uncharacterized mechanism of signal transmission. PubMed: 25018021DOI: 10.1016/j.molcel.2014.06.010 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.64 Å) |
Structure validation
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