3W1G
Crystal Structure of Human DNA ligase IV-Artemis Complex (Native)
Summary for 3W1G
| Entry DOI | 10.2210/pdb3w1g/pdb |
| Related | 1IK9 1X9N 2E2W 3II6 3VNN 3W1B 3W5O |
| Descriptor | DNA ligase 4, Artemis-derived peptide, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | dna ligase, non homologous end joining, dna repair, xrcc4, ligase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P49917 Q96SD1 |
| Total number of polymer chains | 2 |
| Total formula weight | 72939.09 |
| Authors | Ochi, T.,Blundell, T.L. (deposition date: 2012-11-15, release date: 2013-04-03, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 23523427DOI: 10.1016/j.str.2013.02.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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