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. 2024 Aug 30;12:92. doi: 10.1186/s40364-024-00641-6

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — Structures of four members of the human bromodomain and extra-terminal structural domain (BET) family of proteins. All BET proteins have two tandem bromodomains (BD1, BD2) and an extra-terminal structural domain (ET), and the ET structural domains are indicated in pink. There are additional C-terminal domains (CTD), also known as positive transcription elongation factor b (P-TEFb) interaction domain (PID), in the long variant of BRD4 and in the BRDT proteins; CTD structural domains are indicated in orange. The short variant of BRD4 does not have CTD structural domains or histone acetyltransferases (HAT) kinase activity. Additionally, other structural domains were identified in the BRD4 protein, including the N-segment phosphorylation site (NPS), indicated in purple, with an amino acid range of 472–500; the basic residue-enriched structural domain, also known as the basic interaction structural domain (BID), indicated in yellow, with an amino acid range of 524–579; and the C-terminal phosphorylation site (CPS), indicated in green, with an amino acid range of 697–720. Among them, the bromodomain (BD1, BD2) mainly binds to acetylated lysine residues on histones and nonhistone proteins; the ET structural domain mainly mediates interactions with proteins such as transcription factors (TFs); the CTD is mainly responsible for the recruitment of and interaction with P-TEFb; and the NPS is negatively charged, which promotes BD2 binding to acetylated lysine residues, BID is positively charged and can form intramolecular contacts with NPS and inhibit BD2 binding to acetylated lysine residues