3G65

Crystal Structure of the Human Rad9-Rad1-Hus1 DNA Damage Checkpoint Complex

3G65 の概要

• エントリーDOI: 10.2210/pdb3g65/pdb
• 分子名称: Cell cycle checkpoint control protein RAD9A, Cell cycle checkpoint protein RAD1, Checkpoint protein HUS1, ... (4 entities in total)
• 機能のキーワード: pcna, dna binding clamp, dna damage, dna repair, exonuclease, hydrolase, nuclease, nucleus, phosphoprotein, cell cycle
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q99638 O60671 O60921
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 96038.32

構造登録者

Dore, A.S.,Kilkenny, M.L.,Rzechorzek, N.J.,Pearl, L.H. (登録日: 2009-02-06, 公開日: 2009-05-26, 最終更新日: 2023-09-06)

主引用文献

Dore, A.S.,Kilkenny, M.L.,Rzechorzek, N.J.,Pearl, L.H.
Crystal structure of the rad9-rad1-hus1 DNA damage checkpoint complex--implications for clamp loading and regulation.
Mol.Cell, 34:735-745, 2009

PubMed Abstract: Rad9, Rad1, and Hus1 form a heterotrimeric complex (9-1-1) that is loaded onto DNA at sites of DNA damage. DNA-loaded 9-1-1 activates signaling through the Chk1 arm of the DNA damage checkpoint response via recruitment and stimulation of ATR. Additionally, 9-1-1 may play a direct role in facilitating DNA damage repair via interaction with a number of DNA repair enzymes. We have now determined the crystal structure of the human 9-1-1 complex, revealing a toroidal structure with a similar architecture to the homotrimeric PCNA DNA-binding clamp. The structure explains the formation of a unique heterotrimeric arrangement and reveals significant differences among the three subunits in the sites implicated in binding to the clamp loader and to ligand proteins. Biochemical analysis reveals a single repair enzyme-binding site on 9-1-1 that can be blocked competitively by the PCNA-binding cell-cycle regulator p21(cip1/waf1).

PubMed: 19446481
DOI: 10.1016/j.molcel.2009.04.027

実験手法

X-RAY DIFFRACTION (2.9 Å)