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• W2012562829 abstract "Protein recognition of DNA sites is a primary event for gene function. Its ultimate mechanistic understanding requires an integrated structural, dynamic, kinetic, and thermodynamic dissection that is currently limited considering the hundreds of structures of protein-DNA complexes available. We describe a protein-DNA-binding pathway in which an initial, diffuse, transition state ensemble with some nonnative contacts is followed by formation of extensive nonnative interactions that drive the system into a kinetic trap. Finally, nonnative contacts are slowly rearranged into native-like interactions with the DNA backbone. Dissimilar protein-DNA interfaces that populate along the DNA-binding route are explained by a temporary degeneracy of protein-DNA interactions, centered on “dual-role” residues. The nonnative species slow down the reaction allowing for extended functionality." @default.
• W2012562829 created "2016-06-24" @default.
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• W2012562829 date "2010-04-07" @default.
• W2012562829 modified "2023-10-08" @default.
• W2012562829 title "Experimental snapshots of a protein-DNA binding landscape" @default.
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• W2012562829 doi "https://doi.org/10.1073/pnas.0911734107" @default.
• W2012562829 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2867883" @default.
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