title: Modelling the way Ku binds DNA.
abstract: Ku plays a crucial role in the non-homologous end joining pathway to repair DNA double-strand breaks. In this study, we modelled the full-length Ku heterodimer from the truncated crystal structure and NMR structure, and conducted a series of docking and molecular dynamics simulations in an effort to probe the structural, dynamical and energetic features of each domain in free Ku and Ku-DNA complexes.
authors.affiliation: Universities Space Research Association, Division of Space Life Sciences, Houston, TX 77058, USA. shaowen.hu-1@nasa.gov
authors.forename: Shaowen
authors.initials: S
authors.lastname: Hu
authors.forename: Francis A
authors.initials: FA
authors.lastname: Cucinotta
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D004247:DNA / Q000737:chemistry* / Q000648:ultrastructure*; D004265:DNA Helicases / Q000737:chemistry* / Q000648:ultrastructure*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000648:ultrastructure; D000072200:Ku Autoantigen; D008956:Models, Chemical; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D004268:DNA-Binding Proteins; D004247:DNA; D004265:DNA Helicases; C106893:XRCC5 protein, human; D000072200:Ku Autoantigen