3W5O
Crystal Structure of Human DNA ligase IV
Summary for 3W5O
| Entry DOI | 10.2210/pdb3w5o/pdb |
| Related | 1IK9 2E2W 3II6 3VNN 3W1B 3W1G |
| Descriptor | DNA ligase 4, ADENOSINE-5'-TRIPHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | dna ligase, non homologous end joining, dna repair, xrcc4, artemis, ligase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P49917 |
| Total number of polymer chains | 2 |
| Total formula weight | 142396.50 |
| Authors | Gu, X.,Ochi, T.,Blundell, T.L. (deposition date: 2013-02-02, 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 (2.84 Å) |
Structure validation
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