8KCA

Crystal structure of DDX53 helicase domain

8KCA の概要

• エントリーDOI: 10.2210/pdb8kca/pdb
• 分子名称: Probable ATP-dependent RNA helicase DDX53 (2 entities in total)
• 機能のキーワード: rna helicase, rna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44105.64

構造登録者

Park, S.,Yang, J.B.,Jung, H.S.,Kim, H.Y. (登録日: 2023-08-06, 公開日: 2023-08-30, 最終更新日: 2024-05-08)

主引用文献

Park, S.,Yang, J.B.,Park, Y.H.,Kim, Y.K.,Jeoung, D.,Kim, H.Y.,Jung, H.S.
Structural insight into crystal structure of helicase domain of DDX53.
Biochem.Biophys.Res.Commun., 677:190-195, 2023

PubMed Abstract: DEAD box helicase proteins are a family of RNA helicases that participate in various RNA metabolisms such as RNA unwinding, RNA processing, and RNPase activities. A particular DEAD box protein, the DDX53 protein, is primarily expressed in cancer cells and plays a crucial role in tumorigenesis. Numerous studies have revealed that DDX53 interacts with various microRNA and Histone deacetylases. However, its molecular structure and the detailed binding interaction between DDX53 and microRNA or HDAC is still unclear. In this study, we used X-ray crystallography to investigate the 3D structure of the hlicase C-terminal domain of DDX53, and successfully determined its crystal structure at a resolution of 1.97 Å. Subsequently, a functional analysis of RNA was conducted by examining the binding properties thereof with DDX53 by transmission electron microscopy and computing-based molecular docking simulation. The defined 3D model of DDX53 not only provides a structural basis for the fundamental understanding of DDX53 but is also expected to contribute to the field of anti-cancer drug discovery such as structure-based drug discovery and computer-aided drug design.

PubMed: 37603933
DOI: 10.1016/j.bbrc.2023.08.022

実験手法

X-RAY DIFFRACTION (1.97 Å)