3j6j | pdb_00003j6j

3.6 Angstrom resolution MAVS filament generated from helical reconstruction

spinqualitylabelsall models 3j6j, resolution 3.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j6j is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 (CARDMAVS), and requires its interaction with the tandem CARDs of RIG-I (2CARDRIG-I). However, the precise nature of the interaction between 2CARDRIG-I and CARDMAVS, and how this interaction leads to CARDMAVS filament assembly, has been unclear. Here we report a 3.6 A electron microscopy structure of the CARDMAVS filament and a 3.4 A crystal structure of the 2CARDRIG-I:CARDMAVS complex, representing 2CARDRIG-I "caught in the act" of nucleating the CARDMAVS filament. These structures, together with functional analyses, show that 2CARDRIG-I acts as a template for the CARDMAVS filament assembly, by forming a helical tetrameric structure and recruiting CARDMAVS 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. Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I.,Wu B, Peisley A, Tetrault D, Li Z, Egelman EH, Magor KE, Walz T, Penczek PA, Hur S Mol Cell. 2014 Jul 9. pii: S1097-2765(14)00492-4. doi:, 10.1016/j.molcel.2014.06.010. PMID:25018021 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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