1N72

Structure and Ligand of a Histone Acetyltransferase Bromodomain

「1B91」から置き換えられました

1N72 の概要

• エントリーDOI: 10.2210/pdb1n72/pdb
• 分子名称: HISTONE ACETYLTRANSFERASE (1 entity in total)
• 機能のキーワード: histone acetyltransferase bromodomain, 4-helical bundle, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (By similarity): Q92831
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14052.23

構造登録者

Dhalluin, C.,Carlson, J.E.,Zeng, L.,He, C.,Aggarwal, A.K.,Zhou, M.-M. (登録日: 2002-11-12, 公開日: 2002-12-11, 最終更新日: 2024-05-22)

主引用文献

Dhalluin, C.,Carlson, J.E.,Zeng, L.,He, C.,Aggarwal, A.K.,Zhou, M.-M.
Structure and Ligand of a Histone Acetyltransferase Bromodomain
Nature, 399:491-496, 1999

PubMed Abstract: Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.

PubMed: 10365964
DOI: 10.1038/20974

実験手法

SOLUTION NMR