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. 2013 Jan 7;110(4):1458–1463. doi: 10.1073/pnas.1218509110

Fig. 5.

Fig. 5.

Structural comparison around the HA1/HA2 cleavage site of H17 HA with other HAs. (A) GU10-060 HA HA0 cleavage site with HA1 colored green and HA2 colored cyan. Due to flexibility of the cleavage loop, the residues corresponding to HA1 325–329 and HA2 1–5 are not modeled. Overlay around the cleavage loops of H17 HA0 (in green) with H3 HA0 (in brown; PDB ID code 1HA0) (B) and H1 HA0 (in gray; PDB ID code 1RD8) (C). The conformation of modeled putative fusion peptide of H17 is more similar to H3 HA0 than to H1 HA0. For comparison, Fig. 5 AC are generated in the same orientation.

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