1JJR

The Three-Dimensional Structure of the C-terminal DNA Binding Domain of Human Ku70

1JJR の概要

• エントリーDOI: 10.2210/pdb1jjr/pdb
• NMR情報: BMRB: 4941
• 分子名称: THYROID AUTOANTIGEN (1 entity in total)
• 機能のキーワード: dna repair protein, protein-dna interaction, ku70, solution structure, dna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16969.52

構造登録者

Zhang, Z.,Chen, Y. (登録日: 2001-07-09, 公開日: 2001-10-03, 最終更新日: 2024-05-22)

主引用文献

Zhang, Z.,Zhu, L.,Lin, D.,Chen, F.,Chen, D.J.,Chen, Y.
The three-dimensional structure of the C-terminal DNA-binding domain of human Ku70.
J.Biol.Chem., 276:38231-38236, 2001

PubMed Abstract: The proteins Ku70 (69.8 kDa) and Ku80 (82.7 kDa) form a heterodimeric complex that is an essential component of the nonhomologous end joining DNA double-strand break repair pathway in mammalian cells. Interaction of Ku with DNA is central for the functions of Ku. Ku70, which is mainly responsible for the DNA binding activity of the Ku heterodimer, contains two DNA-binding domains. We have solved the solution structure of the Ku80-independent DNA-binding domain of Ku70 encompassing residues 536-609 using nuclear magnetic resonance spectroscopy. Residues 536-560 are highly flexible and have a random structure but form specific interactions with DNA. Residues 561-609 of Ku70 form a well defined structure with 3 alpha-helices and also interact with DNA. The three-dimensional structure indicates that all conserved hydrophobic residues are in the hydrophobic core and therefore may be important for structural integrity. Most of the conserved positively charged residues are likely to be critical for DNA recognition. The C-terminal DNA-binding domain of Ku70 contains a helix-extended strand-helix motif, which occurs in other nucleic acid-binding proteins and may represent a common nucleic acid binding motif.

PubMed: 11457852

実験手法

SOLUTION NMR