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. Author manuscript; available in PMC: 2012 Aug 29.
Published in final edited form as: Nature. 2011 Sep 25;479(7373):423–427. doi: 10.1038/nature10537

Figure 1. Structural overview of RIG-I helicase-RD.

Figure 1

(a, b, and c) Schematic representation of the RIG-I helicase-RD, highlighting the RecA-like domain 1 (blue), the alpha-helical domain 3 (green), RecA-like helicase domain 2 (yellow), and RD (red). The linker connecting Domain 1 with Domain 3 is colored teal, while the V-shape linker between Domain 2 and RD is colored orange. The ADP•BeF3 and dsRNA are shown in stick representation with the 5′ and 3′ strands of the RNA colored black and beige, respectively. A grey sphere denotes the position of the zinc ion in RD. The 3′ and 5′ strands are colored beige and black, respectively. (d, e, f) Surface of RIG-I helicase-RD colored for electrostatic potential at ±5 kT/e; blue (basic), white (neutral), and red (acidic). The views in panels a, b, and c are identical to d, e and f, respectively.