Fig. 2: UB-modified lysines reside in functional domains of the IAV polymerase. | Nature Communications

Fig. 2: UB-modified lysines reside in functional domains of the IAV polymerase.

From: The ubiquitination landscape of the influenza A virus polymerase

Fig. 2

a, b 3D structural models of a WSN-adapted heterotrimeric IAV polymerase bound to vRNA (adapted from PDB: 4WSB; a) or cRNA (adapted from PDB: 5EPI; b) created by comparative homology modeling. Positions of lysines with diglycyl remnants are depicted in violet (PB2, yellow, upper panel), green (PA, violet, middle panel), and magenta (PB1, turquoise, lower panel). c Linear models of PB2 (upper panel), PA (middle panel), and PB1 (lower panel) depicting the location of the identified di-glycylated lysines (K-ε-GG position) in previously described functional domains. Boundaries of functional domains (gray boxes) are depicted in the upper lane (#AA). Interaction sites to viral proteins PA (violet), PB1 (light green), PB2 (orange), NP (dark orange), and NEP (brown) and the cellular proteins pol-II (dark green), importin (bright orange), and ANP32A (pink) are included. RNA interaction sites are depicted as follows: mRNA (gray) vRNA (white boxes) or cRNA (black boxes) and the 5′Cap-structures of cellular mRNAs (bright green boxes). Other functional motives include the catalytic domains of the polymerase in PB1 (light pink), NLS (violet), and the priming loop (dark green).

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