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Cooperative DNA Recognition Modulated by an Interplay between Protein-Protein Interactions and DNA-Mediated Allostery.

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Academic year: 2017

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Fig 1. Interactions and structural changes at the protein-DNA interfaces. (A) The OCT4-SOX2- UTF1 complex
Fig 2. Orientational dynamics in DNA-bound configurations. (A,B) Schematic view of the coordinate system (A) and definition (B) of the Rock and Tumble angles describing the orientation of the docking helices (shown as opaque cartoons) of the two domains of
Fig 3. Correlated motions and allosteric communication pathways. (A,B) Positional cross-correlation between OCT4 and the DNA in the absence (A) or presence (B) of SOX2
Fig 5. Unbinding profiles of the OCT4 domains. The change in the number of protein-DNA contacts is shown during the unbinding simulations while pulling the POU S (A,B) or the POU HD (C-F)
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