3LJW

Crystal Structure of the Second Bromodomain of Human Polybromo

Summary for 3LJW

• Entry DOI: 10.2210/pdb3ljw/pdb
• Descriptor: Protein polybromo-1, ACETATE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: alpha helix, alternative splicing, bromodomain, chromatin regulator, dna-binding, nucleus, phosphoprotein, transcription, transcription regulation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 27320.37

Authors

Charlop-Powers, Z.,Zhou, M.M.,Zeng, L.,Zhang, Q. (deposition date: 2010-01-26, release date: 2010-05-19, Last modification date: 2023-09-06)

Primary citation

Charlop-Powers, Z.,Zeng, L.,Zhang, Q.,Zhou, M.M.
Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2.
Cell Res., 20:529-538, 2010

PubMed Abstract: The Polybromo (PB) protein functions as a key component of the human PBAF chromatin remodeling complex in regulation of gene transcription. PB is made up of modular domains including six bromodomains that are known as acetyl-lysine binding domains. However, histone-binding specificity of the bromodomains of PB has remained elusive. In this study, we report biochemical characterization of all six PB bromodomains' binding to a suite of lysine-acetylated peptides derived from known acetylation sites on human core histones. We demonstrate that bromodomain 2 of PB preferentially recognizes acetylated lysine 14 of histone H3 (H3K14ac), a post-translational mark known for gene transcriptional activation. We further describe the molecular basis of the selective H3K14ac recognition of bromodomain 2 by solving the protein structures in both the free and bound forms using X-ray crystallography and NMR, respectively.

PubMed: 20368734
DOI: 10.1038/cr.2010.43

Experimental method

X-RAY DIFFRACTION (1.501 Å)