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- W2952873921 abstract "Abstract TIP60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and non-histone proteins within diverse cellular processes. Whereas the TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. Here we attempted a quantitative analysis of the interaction between the TIP60-CB and histone peptides, but did not observe any binding through either fluorescence polarization or isothermal titration calorimetry. We solved a crystal structure of the TIP60-CB alone. Analysis of the crystal structure demonstrates a putative peptide binding site that may be occluded by the basic side chain of a residue in a unique β hairpin between the two N-terminal strands of the β barrel." @default.
- W2952873921 created "2019-06-27" @default.
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- W2952873921 date "2018-01-31" @default.
- W2952873921 modified "2023-10-16" @default.
- W2952873921 title "Structural and histone binding studies of the chromo barrel domain of TIP60" @default.
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- W2952873921 doi "https://doi.org/10.1101/257485" @default.
- W2952873921 hasPublicationYear "2018" @default.
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