Selected article for: "card activation and rig activation"
Author: Brisse, Morgan; Ly, Hinh
Title: Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5
  • Document date: 2019_7_17
    • ID: 1enteev7_21
    Snippet: Upon binding to PAMP (dsRNA), RIG-I oligomerizes with other RIG-I/dsRNA complexes to form helical oligomers (128) in a 2:2 complex using the purified RIG-I protein (87) , where the activating ubiquitin motifs serve as a scaffold to link the oligomers together (118) . These oligomers have been found to be necessary under normal conditions to activate RIG-I. This may be due to the helical structure of the RIG-I oligomers closely matching those form.....
    Document: Upon binding to PAMP (dsRNA), RIG-I oligomerizes with other RIG-I/dsRNA complexes to form helical oligomers (128) in a 2:2 complex using the purified RIG-I protein (87) , where the activating ubiquitin motifs serve as a scaffold to link the oligomers together (118) . These oligomers have been found to be necessary under normal conditions to activate RIG-I. This may be due to the helical structure of the RIG-I oligomers closely matching those formed by MAVS (63) , which is known to form filaments in-vitro (129, 130) mediated by its own CARD domains (131, 132) . A structural model of MAVS activation by RIG-I has been proposed of stacking MAVS CARD domains on top of RIG-I CARD domains to extend the RIG-I helix (133) .

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