2GRC

1.5 A structure of bromodomain from human BRG1 protein, a central ATPase of SWI/SNF remodeling complex

2GRC の概要

• エントリーDOI: 10.2210/pdb2grc/pdb
• 分子名称: Probable global transcription activator SNF2L4 (2 entities in total)
• 機能のキーワード: bromodomain, brg1, chromatin remodelling, acely-lysine binding, protein-protein interactions, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : P51532
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15091.30

構造登録者

Singh, M.,Popowicz, G.M.,Krajewski, M.,Holak, T.A. (登録日: 2006-04-24, 公開日: 2007-05-08, 最終更新日: 2024-02-14)

主引用文献

Singh, M.,Popowicz, G.M.,Krajewski, M.,Holak, T.A.
Structural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complex.
Chembiochem, 8:1308-1316, 2007

PubMed Abstract: Bromodomains represent an extensive family of evolutionarily conserved domains that are found in many chromatin-associated proteins such as histone acetyltransferases (HAT) and subunits of ATP-dependent chromatin-remodeling complexes. These domains are associated with acetylated lysine residues that bind both in vivo and in vitro; for example, they bind to the N-acetylated lysines of the histone tail of nucleosomes. In this report, we determined the structure of the bromodomain from human brahma-related gene 1 (BRG1) protein, a subunit of an ATP-dependent switching/sucrose nonfermenting (SWI/SNF) remodeling complex, and have also characterized its in vitro interaction with N-acetylated lysine peptides from histones. In addition to a typical all-alpha-helical fold that was observed in the bromodomains, we observed for the first time a small beta-sheet in the ZA loop region of the BRG1 protein. The BRG1 bromodomain exhibited binding, albeit weak, to acetylated peptides that were derived from histones H3 and H4. We have compared the acetyl-lysine binding sites of BRG1 bromodomain with the yGCN5 (general control of amino acid biosynthesis). By modeling the acetylated-lysine peptide into the BRG1 bromodomain structure, we were able to explain the weak binding of acetylated-lysine peptides to this bromodomain.

PubMed: 17582821
DOI: 10.1002/cbic.200600562

実験手法

X-RAY DIFFRACTION (1.5 Å)