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. 2013 Aug;19(28):5051–5064. doi: 10.2174/13816128113199990382

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© Bentham Science Publishers

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. (2) — Structure of KAT3 proteins. CBP and p300 share a number of structural domains including three cysteine/histidine rich regions (CH1-CH3) for protein-protein interaction, the KIX domain that mediates the interaction with CREB and other transcription factors, and the KAT domain. The domains of highest homology and the percentage of amino acid identity between the two proteins are indicated. Regions of high homology between the human CBP and p300 proteins expressed as % identity. NRID, nuclear hormone receptor interacting domain; CH1-3, cysteine/histidine-rich regions 1-3; TAZ1-2, transcriptional adaptor Zn-finger domain 1-2; KIX, kinase inducible domain; Br, bromodomain; PHD, plant homeodomain; ZZ, ZZ-type Zn-finger domain; SID, SRC- 1 interacting domain; MDM2, p53 E3-ubiquitin protein ligase homolog; ATF, activation transcription factors; TBP, TATA-binding protein. Figure modified from [52].