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Molecular mechanisms of cooperative binding of transcription factors Runx1–CBFβ–Ets1 on the TCRα gene enhancer

Fig 3

Changes in DNA conformations around the G4–C112 base-pair.

(A) 3D structures of the G4–C112 base-pair taken from the three simulations: the wild-type quaternary complex (red), the quaternary complex with the Runx1 K167A mutant (green), and the isolated DNA (purple). The snapshots were taken at the times when the X-displacement parameter was near the average value for each model. The three structures are superimposed, based on the adjacent base-pair (A3–T113; the thin lines). (B) The averages and standard deviations of the X-displacement parameter in the wild-type quaternary complex (red), the Ets1–DNA complex (blue), the isolated DNA (purple), the quaternary complex with Runx1 K167A mutant (green), and the quaternary complex with Ets1 Y329A mutant (cyan).

Fig 3

doi: https://doi.org/10.1371/journal.pone.0172654.g003