A structure-based model of RIG-I activation.

By D. Kolakofsky, E. Kowalinski, Stephen Cusack. 2012

152 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

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In Immunology

In Molecular Biology

Citations in the corpus

The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands (2022, neutral): “RIG-I displays exquisite sensitivity in recognizing minute quantities of viral RNA in the cytoplasm and then forming a tight RNA:protein complex that releases specialized signaling domains (CARDs, or caspase recruitment domains), which engage in a cascade of downstream interactions leading to the in”
Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5 (2015, unknown): “RIG-I or MDA5 CARDs, which are released upon cognate RNA binding, mediate signal transduction by interacting with the CARD of the membrane-bound mitochondrial antiviral signaling (MAVS) adaptor [1, 11–14].”
Structural basis for m7G recognition and 2′-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I (2016, unknown): “Therefore, the discrepancy between the current 5′ppp structure and 4AY2 is likely due to the presence of a disulfide bond in the Hel2i of 4AY2, different crystallization conditions, or different crystal packing arrangement (16, 17).”
Establishing the role of ATP for the function of the RIG-I innate immune sensor (2015, background): “Alignment of RIG-I in an apo conformation (PDB 4A2W) to structures of RIG-I bound only to RNA (PDB 4AY2) or bound to RNA and the ATP analog ADP-AlF4 (PDB 4A36) show that the CARDs of RIG-I can be accommodated in apo and RNA-bound states, but not when bound to both RNA and the ATP analog (Jiang et al”
Defining the functional determinants for RNA surveillance by RIG-I (2013, unknown): “While polyubiquitin mediated oligomerization of the CARD domains is required for interferon production [15,27], the oligomerization state and the functional stoichiometry of the RIG-I:RNA complex is not well understood [28].”
A minimal RNA ligand for potent RIG-I activation in living mice (2017, background): “Structural studies, quantitative biochemical work, cell-based assays and imaging studies have all established that RIGI is an “RNA end-capper” that encircles a 10-base-pair RNA duplex as a monomer and forms a network of specific interactions with the terminal base-pair and the 5’triphosphate (3, 10-”
RNA binding activates RIG-I by releasing an autorepressed signaling domain (2019, background): “Careful in vitro investigation of PRRs and their ligands is necessary to complement cell-based results and has led to notable advances in our understanding of RIG-I (8, 9).”
Influenza A Virus Panhandle Structure Is Directly Involved in RIG-I Activation and Interferon Induction (2015, background): “dent and does not require full complementarity (53).”