Fig. 2: H5N1 FluPolA dimer forms a replication platform with human ANP32B. | Nature Communications

Fig. 2: H5N1 FluPolA dimer forms a replication platform with human ANP32B.

From: Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation

Fig. 2: H5N1 FluPolA dimer forms a replication platform with human ANP32B.

a Cryo-EM map of IAV replication platform composed of a replicase heterotrimer (FluPolR, blue), an encapsidating heterotrimer (FluPolE, green) and ANP32BLRR (orange). b Model showing the organisation of the PB2 flexible domains and PAEndo in the replication platform. c Close-up view of the PAEndo, PB2Lid and PB2CBD interface. d–f Close-up views of the FluPolR-FluPolE interface. g Close-up view of the PB2627-ANP32B interface. Dashed lines indicate hydrogen bonds. For panel c–g, the dashed rectangles in panels a and b denote the close-up view position. h Electrostatic iso-surface of the FluPolE PB2627-NLS–FluPolR PB2627 domains showing a positively charged groove adjacent to ANP32BLRR, with the dashed line highlighting the putative path of the ANP32LCAR domain. The orientation is identical to the rotated view in panel (b).

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