Fig. 1
From: Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
Oligomeric state of NS1 and identification of TRIM25-interacting domains. a Schematic representation of TRIM25, NS1 and RIG-I domain structures. The crystallised TRIM25 CC-PRYSPRY domain is highlighted in blue and the crystallised RBD and NS1 domains of NS1 in red. The tandem CARD construct of RIG-I used in substrate ubiquitination assays is highlighted in purple. b The effect of different mutations on the oligomeric state of NS1-FL assessed by SEC–MALLS. The traces are colour coded according to the NS1 mutant and concentration used. c Quantification of the TRIM25-CC interaction with NS1 by biolayer interferometry (BLI). The binding curves are colour-coded and Kds determined are listed. The error is the standard deviation (s.d.) of mean from at least three independent experiments
