4HTP

Crystal structure of the DBD domain of human DNA ligase IV bound to Artemis peptide

4HTP の概要

• エントリーDOI: 10.2210/pdb4htp/pdb
• 分子名称: DNA ligase 4, Protein artemis (3 entities in total)
• 機能のキーワード: helical domain, dna binding domain, dna, artemis, ligase-hydrolase complex, ligase/hydrolase
• 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: 4
• 化学式量合計: 57596.63

構造登録者

De Ioannes, P.E.,Aggarwal, A.K. (登録日: 2012-11-01, 公開日: 2012-12-26, 最終更新日: 2024-10-09)

主引用文献

De Ioannes, P.,Malu, S.,Cortes, P.,Aggarwal, A.K.
Structural Basis of DNA Ligase IV-Artemis Interaction in Nonhomologous End-Joining.
Cell Rep, 2:1505-1512, 2012

PubMed Abstract: DNA ligase IV (LigIV) and Artemis are central components of the nonhomologous end-joining (NHEJ) machinery that is required for V(D)J recombination and the maintenance of genomic integrity in mammalian cells. We report here crystal structures of the LigIV DNA binding domain (DBD) in both its apo form and in complex with a peptide derived from the Artemis C-terminal region. We show that LigIV interacts with Artemis through an extended hydrophobic surface. In particular, we find that the helix α2 in LigIV-DBD is longer than in other mammalian ligases and presents residues that specifically interact with the Artemis peptide, which adopts a partially helical conformation on binding. Mutations of key residues on the LigIV-DBD hydrophobic surface abolish the interaction. Together, our results provide structural insights into the specificity of the LigIV-Artemis interaction and how the enzymatic activities of the two proteins may be coordinated during NHEJ.

PubMed: 23219551
DOI: 10.1016/j.celrep.2012.11.004

実験手法

X-RAY DIFFRACTION (2.2502 Å)