3VNN

Crystal Structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of human DNA ligase IV

3VNN の概要

• エントリーDOI: 10.2210/pdb3vnn/pdb
• 関連するPDBエントリー: 1IK9 1X9N 2E2W 3II6 3L2P
• 分子名称: DNA ligase 4 (2 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)
• 細胞内の位置: Nucleus: P49917
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16196.51

構造登録者

Ochi, T.,Wu, Q.,Chirgadze, D.Y.,Grossmann, J.G.,Bolanos-Garcia, V.M.,Blundell, T.L. (登録日: 2012-01-17, 公開日: 2012-06-20, 最終更新日: 2024-03-20)

主引用文献

Ochi, T.,Wu, Q.,Chirgadze, D.Y.,Grossmann, J.G.,Bolanos-Garcia, V.M.,Blundell, T.L.
Structural insights into the role of domain flexibility in human DNA ligase IV
Structure, 20:1212-1222, 2012

PubMed Abstract: Knowledge of the architecture of DNA ligase IV (LigIV) and interactions with XRCC4 and XLF-Cernunnos is necessary for understanding its role in the ligation of double-strand breaks during nonhomologous end joining. Here we report the structure of a subdomain of the nucleotidyltrasferase domain of human LigIV and provide insights into the residues associated with LIG4 syndrome. We use this structural information together with the known structures of the BRCT/XRCC4 complex and those of LigIV orthologs to interpret small-angle X-ray scattering of LigIV in complex with XRCC4 and size exclusion chromatography of LigIV, XRCC4, and XLF-Cernunnos. Our results suggest that the flexibility of the catalytic region is limited in a manner that affects the formation of the LigIV/XRCC4/XLF-Cernunnos complex.

PubMed: 22658747
DOI: 10.1016/j.str.2012.04.012

実験手法

X-RAY DIFFRACTION (2.903 Å)