2KTB

Solution Structure of the Second Bromodomain of Human Polybromo in complex with an acetylated peptide from Histone 3

Summary for 2KTB

• Entry DOI: 10.2210/pdb2ktb/pdb
• NMR Information: BMRB: 16694
• Descriptor: H3_Peptide, Protein polybromo-1 (2 entities in total)
• Functional Keywords: bromodomain, alternative splicing, chromatin regulator, dna-binding, nucleus, phosphoprotein, transcription, transcription regulation, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q86U86
• Total number of polymer chains: 2
• Total formula weight: 15908.33

Authors

Charlop-Powers, Z.,Zhang, Q.,Zeng, L. (deposition date: 2010-01-26, release date: 2010-05-12, Last modification date: 2024-11-06)

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

SOLUTION NMR