2RNX
The Structural Basis for Site-Specific Lysine-Acetylated Histone Recognition by the Bromodomains of the HUman Transcriptional Co-Activators PCAF and CBP
Summary for 2RNX
| Entry DOI | 10.2210/pdb2rnx/pdb |
| Related | 2RNW |
| Descriptor | Histone acetyltransferase PCAF, Histone H3 (2 entities in total) |
| Functional Keywords | bromodomain, histone, acetyltransferase, acyltransferase, cell cycle, host-virus interaction, nucleus, polymorphism, transcription, transcription regulation, acetylation, chromosomal protein, dna damage, dna repair, dna-binding, methylation, nucleosome core, phosphoprotein, transferase-nuclear protein complex, transferase/nuclear protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus (By similarity): Q92831 Nucleus: P61830 |
| Total number of polymer chains | 2 |
| Total formula weight | 15559.00 |
| Authors | Zeng, L.,Zhang, Q.,Gerona-Navarro, G.,Zhou, M.M. (deposition date: 2008-02-03, release date: 2008-05-06, Last modification date: 2023-11-15) |
| Primary citation | Zeng, L.,Zhang, Q.,Gerona-Navarro, G.,Moshkina, N.,Zhou, M.M. Structural Basis of Site-Specific Histone Recognition by the Bromodomains of Human Coactivators PCAF and CBP/p300 Structure, 16:643-652, 2008 Cited by PubMed Abstract: Histone lysine acetylation is central to epigenetic control of gene transcription. Bromodomains of chromosomal proteins function as acetyl-lysine (Kac) binding domains. However, how bromodomains recognize site-specific histones remains unanswered. Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. From structural and biochemical binding analyses, we determine consensus histone recognition by the bromodomains of PCAF and CBP, which represent two different subgroups of the bromodomain family. Through bromodomain residues in the ZA and BC loops, PCAF prefers acetylation sites with a hydrophobic residue at (Kac+2) position and a positively charged or aromatic residue at (Kac+3), whereas CBP favors bulky hydrophobic residues at (Kac+1) and (Kac+2), a positively charged residue at (Kac-1), and an aromatic residue at (Kac-2). PubMed: 18400184DOI: 10.1016/j.str.2008.01.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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