4AV1

Crystal structure of the human PARP-1 DNA binding domain in complex with DNA

4AV1 の概要

• エントリーDOI: 10.2210/pdb4av1/pdb
• 関連するPDBエントリー: 1UK0 1UK1 1WOK 2COK 2CR9 2CS2
• 分子名称: POLY [ADP-RIBOSE] POLYMERASE 1, 5'-D(*AP*AP*GP*TP*GP*TP*TP*GP*CP*AP*TP*TP)-3', 5'-D(*TP*AP*AP*TP*GP*CP*AP*AP*CP*AP*CP*TP)-3', ... (5 entities in total)
• 機能のキーワード: transferase, parp1, dna-binding domain, dbd, dna repair, cancer, poly- adp(ribosyl)ation
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: P09874
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 107959.48

構造登録者

Ali, A.A.E.,Timinszky, G.,Arribas-Bosacoma, R.,Kozlowski, M.,Hassa, P.O.,Hassler, M.,Ladurner, A.G.,Pearl, L.H.,Oliver, A.W. (登録日: 2012-05-23, 公開日: 2012-06-13, 最終更新日: 2024-05-01)

主引用文献

Ali, A.A.E.,Timinszky, G.,Arribas-Bosacoma, R.,Kozlowski, M.,Hassa, P.O.,Hassler, M.,Ladurner, A.G.,Pearl, L.H.,Oliver, A.W.
The Zinc-Finger Domains of Parp1 Cooperate to Recognise DNA Strand-Breaks
Nat.Struct.Mol.Biol., 19:685-, 2012

PubMed Abstract: Poly(ADP-ribose) polymerase 1 (PARP1) is a primary DNA damage sensor whose (ADP-ribose) polymerase activity is acutely regulated by interaction with DNA breaks. Upon activation at sites of DNA damage, PARP1 modifies itself and other proteins by covalent addition of long, branched polymers of ADP-ribose, which in turn recruit downstream DNA repair and chromatin remodeling factors. PARP1 recognizes DNA damage through its N-terminal DNA-binding domain (DBD), which consists of a tandem repeat of an unusual zinc-finger (ZnF) domain. We have determined the crystal structure of the human PARP1-DBD bound to a DNA break. Along with functional analysis of PARP1 recruitment to sites of DNA damage in vivo, the structure reveals a dimeric assembly whereby ZnF1 and ZnF2 domains from separate PARP1 molecules form a strand-break recognition module that helps activate PARP1 by facilitating its dimerization and consequent trans-automodification.

PubMed: 22683995
DOI: 10.1038/NSMB.2335

実験手法

X-RAY DIFFRACTION (3.1 Å)