3W1B

Crystal Structure of Human DNA ligase IV-Artemis Complex (Mercury Derivative)

3W1B の概要

• エントリーDOI: 10.2210/pdb3w1b/pdb
• 関連するPDBエントリー: 1IK9 1X9N 2E2W 3II6 3L2P 3VNN 3W1G 3W5O
• 分子名称: DNA ligase 4, Artemis-derived peptide, ADENOSINE MONOPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: dna ligase, non-homologous end joining, dna repair, xrcc4, ligase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P49917 Q96SD1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74104.13

構造登録者

Ochi, T.,Blundell, T.L. (登録日: 2012-11-14, 公開日: 2013-04-03, 最終更新日: 2024-10-16)

主引用文献

Ochi, T.,Gu, X.,Blundell, T.L.
Structure of the catalytic region of DNA ligase IV in complex with an artemis fragment sheds light on double-strand break repair
Structure, 21:672-679, 2013

PubMed Abstract: Nonhomologous end joining (NHEJ) is central to the repair of double-stranded DNA breaks throughout the cell cycle and plays roles in the development of the immune system. Although three-dimensional structures of most components of NHEJ have been defined, those of the catalytic region of DNA ligase IV (LigIV), a specialized DNA ligase known to work in NHEJ, and of Artemis have remained unresolved. Here, we report the crystal structure at 2.4 Å resolution of the catalytic region of LigIV (residues 1-609) in complex with an Artemis peptide. We describe interactions of the DNA-binding domain of LigIV with the continuous epitope of Artemis, which, together, form a three-helix bundle. A kink in the first helix of LigIV introduced by a conserved VPF motif gives rise to a hydrophobic pocket, which accommodates a conserved tryptophan from Artemis. We provide structural insights into features of LigIV among human DNA ligases.

PubMed: 23523427
DOI: 10.1016/j.str.2013.02.014

実験手法

X-RAY DIFFRACTION (2.4 Å)