1IK9

CRYSTAL STRUCTURE OF A XRCC4-DNA LIGASE IV COMPLEX

1IK9 の概要

• エントリーDOI: 10.2210/pdb1ik9/pdb
• 分子名称: DNA REPAIR PROTEIN XRCC4, DNA LIGASE IV (3 entities in total)
• 機能のキーワード: dna end joining, double-strand break repair, v(d)j recombination, protein-protein complex, coiled coil, gene regulation-ligase complex, gene regulation/ligase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q13426 P49917
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53256.92

構造登録者

Sibanda, B.L.,Critchlow, S.E.,Begun, J.,Pei, X.Y.,Jackson, S.P.,Blundell, T.L.,Pellegrini, L. (登録日: 2001-05-03, 公開日: 2001-11-21, 最終更新日: 2024-02-07)

主引用文献

Sibanda, B.L.,Critchlow, S.E.,Begun, J.,Pei, X.Y.,Jackson, S.P.,Blundell, T.L.,Pellegrini, L.
Crystal structure of an Xrcc4-DNA ligase IV complex.
Nat.Struct.Biol., 8:1015-1019, 2001

PubMed Abstract: A complex of two proteins, Xrcc4 and DNA ligase IV, plays a fundamental role in DNA non-homologous end joining (NHEJ), a cellular function required for double-strand break repair and V(D)J recombination. Here we report the crystal structure of human Xrcc4 bound to a polypeptide that corresponds to the DNA ligase IV sequence linking its two BRCA1 C-terminal (BRCT) domains. In the complex, a single ligase chain binds asymmetrically to an Xrcc4 dimer. The helical tails of Xrcc4 undergo a substantial conformational change relative to the uncomplexed protein, forming a coiled coil that unwinds upon ligase binding, leading to a flat interaction surface. A buried network of charged hydrogen bonds surrounded by extensive hydrophobic contacts explains the observed tightness of the interaction. The strong conservation of residues at the interface between the two proteins provides evidence that the observed mode of interaction has been maintained in NHEJ throughout evolution.

PubMed: 11702069
DOI: 10.1038/nsb725

実験手法

X-RAY DIFFRACTION (2.3 Å)