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cc-by-nc-nd (c) Elsevier Ltd, 2019
Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/153994

How B-DNA dynamics decipher sequence-selective protein recognition

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The rules governing sequence-specific DNA-protein recognition are under a long-standing debate regarding the prevalence of base versus shape readout mechanisms to explain sequence specificity and of the conformational selection versus induced fit binding paradigms to explain binding-related conformational changes in DNA. Using a combination of atomistic simulations on a subset of representative sequences and mesoscopic simulations at the protein-DNA interactome level, we demonstrate the prevalence of the shape readout model in determining sequence-specificity and of the conformational selection paradigm in defining the general mechanism for binding-related conformational changes in DNA. Our results suggest that the DNA uses a double mechanism to adapt its structure to the protein: it moves along the easiest deformation modes to approach the bioactive conformation, while final adjustments require localized rearrangements at the base-pair step and backbone level. Our study highlights the large impact of B-DNA dynamics in modulating DNA-protein binding.

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BATTISTINI, Federica, HOSPITAL, Adam, BUITRAGO OSPINA, Diana camila, GALLEGO PEREZ, Diego, DANS, Pablo d., GELPÍ BUCHACA, Josep lluís, OROZCO LÓPEZ, Modesto. How B-DNA dynamics decipher sequence-selective protein recognition. _Journal of Molecular Biology_. 2019. Vol. 431, núm. 3845-3859. [consulta: 24 de gener de 2026]. ISSN: 0022-2836. [Disponible a: https://hdl.handle.net/2445/153994]

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