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Figure 3 | Retrovirology

Figure 3

From: Computational modeling suggests dimerization of equine infectious anemia virus Rev is required for RNA binding

Figure 3

Structural features of Rev models. A. Cartoon representations of the top-scoring elongated and globular models for each of the four EIAV Rev sequences analyzed. The elongated models share a similar overall fold, with the defining structural feature being an extended alpha helix in the central region (colored yellow). The globular models are defined by a ‘hinged’ fold, wherein the central region is disrupted by a kink, indicated by black arrows. The color code used for visualizing the models is shown below in the context of the domain structure of Rev165. B. Relative positioning of ARM-1 and ARM-2 in top scoring elongated and globular Rev165 models, showing three different rotational angles. In all three angles, ARM-1 and ARM-2 are well separated in the tertiary structure, and are on opposite faces. C. Electrostatic surface representation corresponding to the right-most rotational view of Rev165 shown in Figure 3B. Negative charges on the protein surface are colored red and positive charges are colored blue. The patch of positive charge bridging ARM-1 and ARM-2 consists of residues from exon1, which can be deleted with no effect on Rev function in vivo.

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