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. 2008 Jun 6;283(23):15825–15833. doi: 10.1074/jbc.M800542200

FIGURE 5.

FIGURE 5.

A comparison of LGP2 structure to the Hef helicase domain. A, a comparison of the overall structures of the LGP2 and the Hef helicase domain (Protein Data Bank code 1WP9) and the C-terminal RIG-I regulatory domain (green) (Protein Data Bank code 2QFB). B–E, results from manual docking of Hhd and the RIG-I RD into the LGP2 electron shell. The orientations of the views relative to each other are indicated by the arrows. The helicase motifs of Hhd are colored in pink and fit nicely into the grooved part of the LGP2 reconstruction. The RD of RIG-I is in green, and the eight RNA-binding residues identified in Refs. 15 and 16 are in yellow. Two of the highlighted residues are in the surface away from the helicase motifs, as shown in D. It is possible that the observed effects of these two residues on RNA binding identified in Ref. 16 are due to an indirect effect of the presence of RNA.