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Bromodomain Interactions with Acetylated Histone 4 Peptides in the BRD4 Tandem Domain: Effects on Domain Dynamics and Internal Flexibility.

Author: AkkeMikael, BobbyRomel, EmbreyKevin J, FlavellLiz, HoldgateGeoffrey A, MilbradtAlexander G, WernerssonSven

Journal ArticleAn article published in an academic or professional journal that reports original research or scholarly analysis.
Research Support, Non-U.S. Gov'tResearch funding provided by government agencies outside the United States.

Overview

This study investigated the dynamics and interactions of the bromodomain and extra-terminal (BET) protein BRD4 using nuclear magnetic resonance (NMR) spectroscopy. It was found that the two bromodomains, BD1 and BD2, have different dynamics and dimerization propensities, which may influence their interactions with target proteins and ligands. The study provides insights into target recognition by BRD4.
Paper Details　
Original Abstract of the Article :
The bromodomain and extra-terminal (BET) protein BRD4 regulates gene expression via recruitment of transcriptional regulatory complexes to acetylated chromatin. Like other BET proteins, BRD4 contains two bromodomains, BD1 and BD2, that can interact cooperatively with target proteins and designed lig...See full text at original site
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引用元：
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9631989/

データ提供：米国国立医学図書館（NLM）

BRD4 Bromodomains: Understanding Their Interactions with Acetylated Histone 4

The world of molecular biology is a complex and fascinating landscape. This research delves into the intricate interactions between the bromodomains of the BRD4 protein and acetylated histone 4 peptides. The study utilizes nuclear magnetic resonance spectroscopy to investigate the dynamics and interactions of these molecules. The authors discovered that the peptide affinity for both domains in the tandem construct is lower than for the isolated domains. This research sheds light on the complex dance between these molecules, offering valuable insights into the mechanisms of gene regulation and the potential for targeted drug development.

Unraveling the Secrets of Gene Regulation

This study sheds light on the complex interplay between BRD4 bromodomains and acetylated histone 4 peptides, revealing valuable insights into the mechanisms of gene regulation. The research provides a foundation for understanding target recognition by BRD4, potentially opening new avenues for targeted drug development to modulate gene expression.

Navigating the Labyrinth of Gene Regulation

This research highlights the complexity of gene regulation, emphasizing the importance of understanding the intricate interactions between proteins and DNA. The study's findings offer valuable insights into the mechanisms of gene regulation, potentially paving the way for new therapies that target specific genes involved in various diseases.

Dr.Camel's Conclusion

This research delves deep into the intricate world of molecular biology, exploring the complex interactions between BRD4 bromodomains and acetylated histone 4 peptides. The study's findings offer valuable insights into the mechanisms of gene regulation, potentially opening new avenues for targeted drug development to modulate gene expression. This research reminds us that the desert of molecular biology is vast and full of hidden treasures waiting to be discovered.

Date :
  1. Date Completed 2022-11-02
  2. Date Revised 2022-12-08
Further Info :

Pubmed ID

36215732

DOI: Digital Object Identifier

PMC9631989

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Languages

English

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