Fig. 6

Model for suppression of substrate ubiquitination by NS1. Model of TRIM25 activity highlighting how the RING domains either side of the anti-parallel CC bind back to dimerise in an intramolecular fashion and come into close proximity of the substrate-binding PRYSPRY domain. The monomers of dimeric TRIM25 are shown in light and dark blue, with ubiquitin-loaded E2 (E2-Ub) in grey and yellow bound to each RING domain while the tandem CARDs of RIG-I (in purple) are bound to the PRYSPRY domain (in green cyan) of TRIM25. The linker connecting the CC and PRYSPRY domain is highlighted in yellow. Binding of NS1 (in red) to the CC of TRIM25 interferes with the linker position and hence correct arrangement of the PRYSPRY domain with respect to the RING domains to suppress substrate ubiquitination