8G7U
Cryo-EM structure of Riplet:RIG-I:dsRNA complex (end-semi-closed end)
Summary for 8G7U
| Entry DOI | 10.2210/pdb8g7u/pdb |
| EMDB information | 29824 |
| Descriptor | Antiviral innate immune response receptor RIG-I, E3 ubiquitin-protein ligase RNF135, p3dsRNA24a, ... (5 entities in total) |
| Functional Keywords | ribonucleoprotein complex, rna sensor, rig-i like receptor, ubiquitination, e3 ligase, trim family, antiviral protein, transferase-hydrolase-rna complex, transferase/hydrolase/rna |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 325178.67 |
| Authors | Wang, W.,Pyle, A.M. (deposition date: 2023-02-17, release date: 2023-11-15, Last modification date: 2024-10-23) |
| Primary citation | Wang, W.,Gotte, B.,Guo, R.,Pyle, A.M. The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization. Nat Commun, 14:7308-7308, 2023 Cited by PubMed Abstract: RIG-I is an essential innate immune receptor that responds to infection by RNA viruses. The RIG-I signaling cascade is mediated by a series of post-translational modifications, the most important of which is ubiquitination of the RIG-I Caspase Recruitment Domains (CARDs) by E3 ligase Riplet. This is required for interaction between RIG-I and its downstream adapter protein MAVS, but the mechanism of action remains unclear. Here we show that Riplet is required for RIG-I signaling in the presence of both short and long dsRNAs, establishing that Riplet activation does not depend upon RIG-I filament formation on long dsRNAs. Likewise, quantitative Riplet-RIG-I affinity measurements establish that Riplet interacts with RIG-I regardless of whether the receptor is bound to RNA. To understand this, we solved high-resolution cryo-EM structures of RIG-I/RNA/Riplet complexes, revealing molecular interfaces that control Riplet-mediated activation and enabling the formulation of a unified model for the role of Riplet in signaling. PubMed: 37951994DOI: 10.1038/s41467-023-42982-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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