2KTB

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

2KTB の概要

• エントリーDOI: 10.2210/pdb2ktb/pdb
• NMR情報: BMRB: 16694
• 分子名称: H3_Peptide, Protein polybromo-1 (2 entities in total)
• 機能のキーワード: bromodomain, alternative splicing, chromatin regulator, dna-binding, nucleus, phosphoprotein, transcription, transcription regulation, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q86U86
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15908.33

構造登録者

Charlop-Powers, Z.,Zhang, Q.,Zeng, L. (登録日: 2010-01-26, 公開日: 2010-05-12, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

SOLUTION NMR