Fig. 3 | Nature Communications

Fig. 3

From: Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition

Fig. 3

Crystal structure of NS1-FL in complex with TRIM25-CC. a The asymmetric unit contains four molecules of each, NS1-FL (R38A/K41A/W187A) and TRIM25-CC, with electron density visible for 2 TRIM25-CC dimers (in dark and light blue), 2 NS1-FL (in red and pink) and 2 NS1-ED domains (in wheat). b NS1-FL resembles the shape of letter Y, with the RBD forming a homodimeric 6-helical structure and the effector domains extending outwards without making contact with each other or the RBDs. c Structural alignment of dimeric NS1-FL from a using the RBD for the overlap shows that the two protomers are not in identical positions, with one ED being shifted by 17 Å in relation to the other. d Structural alignment of NS1 shown in b (in red) with the other two available apo-NS1-FL structures (A/Vietnam/1203/2004(H5N1), R38A/K41A) shown in yellow (PDB: 3F5T) and (A/MN/993/1980(H6N6) R38A/K41A) shown in blue (PDB: 4OPH) reveals structural flexibility owing to the linker region (LR) of NS1

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