Selected article for: "MAVS domain interact and RIG interact"

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_26
    Snippet: Once fully activated and oligomerized, the RIG-I CARD domain can then interact with MAVS (146) (147) (148) (149) (Figures 4E,I) , which is part of a protein complex containing a variety of other cellular proteins (6) (7) (8) (9) . While the MDA5 CARD domain has much weaker direct association with MAVS than the RIG-I CARD domain, it is sufficient to lead to its activation and potentiates activation of MAVS by RIG-I (146), the mechanisms of which h.....
    Document: Once fully activated and oligomerized, the RIG-I CARD domain can then interact with MAVS (146) (147) (148) (149) (Figures 4E,I) , which is part of a protein complex containing a variety of other cellular proteins (6) (7) (8) (9) . While the MDA5 CARD domain has much weaker direct association with MAVS than the RIG-I CARD domain, it is sufficient to lead to its activation and potentiates activation of MAVS by RIG-I (146), the mechanisms of which have yet to be determined. The activated MAVS complex then initiates a molecular cascade which eventually results in expression of IFN1 (150) (Figure 2) .

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