期刊
FEBS LETTERS
卷 584, 期 18, 页码 3901-3908出版社
WILEY
DOI: 10.1016/j.febslet.2010.08.013
关键词
BET family; Bromodomain; Cell cycle; Chromatin; Crystal structure; Papilloma virus; Transcription
资金
- National Institute of Biomedical Innovation (NIBIO) of Japan
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan [19790083, 22790101]
- RIKEN Structural Genomics/Proteomics Initiative (RSGI)
- MEXT
- Grants-in-Aid for Scientific Research [19790083, 22790101] Funding Source: KAKEN
The BET family proteins recognize acetylated chromatin through their two bromodomains, acting as transcriptional activators or tethering viral genomes to the mitotic chromosomes of their host. The structural mechanism for how the N-terminal bromodomain of human BRD2 (BRD2-BD1) deciphers the mono-acetylated status of histone H4 tail was recently reported. Here we show the crystal structure of the second bromodomain of BRD2 (BRD2-BD2) in complex with the di-acetylated histone H4 tail (H4K5ac/K12ac). To our surprise, a single K5ac/K12ac peptide interacts with two BRD2-BD2 molecules simultaneously:the K5ac residue binds to one BRD2-BD2 molecule while the K12ac residue binds to another. These results provide a structural basis for the recognition of two different patterns of the histone acetylation status by a single bromodomain. Structured summary: MINT-7989882, MINT-7989824, MINT-7989846, MINT-7989865:H4 (uniprotkb:P62805) binds (MI:0407) to BRD2 (uniprotkb:P25440) by surface plasmon resonance (MI:0107) MINT-7989539: H4 (uniprotkb:P62805) and BRD2 (uniprotkb:P25440) bind (MI:0407) by X-ray crystallography (MI:0114) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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