Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair

By J. Walker, R. A. Corpina, J. Goldberg. Nature, 2001

1,255 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/dc1f97a0309e47f3de26f17c9e7475ee5e9c8579

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In Molecular Biology

Citations in the corpus

Gene targeting in filamentous fungi: the benefits of impaired repair (2007, background): “Solving the three-dimensional structure of the mammalian Ku complex revealed its toroidal shape that contains positively charged amino acids inside an asymmetrical ring (Walker et al. 2001).”
Mechanism and regulation of class switch recombination. (2008, background): “Ku70–Ku80 forms a ring with a broad base that encircles DNA and can only dissociate at an end (176).”
Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA (2016, background): “The Ku70-Ku80 hetero-dimer is involved in DNA double-strand break repair and the βbarrel domain contributes to DNA binding [18].”
Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis. (2004, methodology): “(C) Lysine residues in the C-terminal linker and DNA-contacting loop of Ku70 that are targeted for acetylation in vivo, superimposed on a ribbon diagram of Ku70/Ku80 based on a crystal structure (Walker et al., 2001).”
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. (2011, background): “Structural studies have shown that Ku70 and Ku80 form a ring-shaped heterodimer that encircles DNA and threads onto DNA by way of a DSB terminus (Walker et al. 2001), while the MRN complex binds DSBs via a globular head region comprised of MRE11 together with joined RAD50 ATPase domains, with MRE11 ”
ATM, ATR, and DNA-PK: The Trinity at the Heart of the DNA Damage Response. (2017, background): “The crystal structure of the Ku heterodimer revealed it tobebasket shaped,withacentral cavity that accommodates a dsDNA end (Walker et al., 2001).”
Chapter 1. General introduction (2015, neutral): “and 80kDa subunit, termed Ku70 and Ku80 respectively (29).”
The Mechanism of Double-Strand DNA Break Repair by the Nonhomologous DNA End Joining Pathway (2010, background): “The crystal structure for Ku lacks the C-terminal 19 kDa [167 amino acids (aa)] of Ku86 (an important region of interaction with DNA-PKcs and other proteins), and this may be a region for conformational change upon Ku binding to DNA (36).”
Protection of mammalian telomeres (2002, background): “…an interaction with TRF1 (Hsu et al., 2000) or TRF2 (Song et al., 2000) but it is also possible that it loads directly onto the chromosome end, since Ku is an endloading ring (Walker et al., 2001) and TTAGGG repeat termini are an adequate substrate for this protein (Bianchi and de Lange, 1999).”
Regulation and mechanisms of mammalian double-strand break repair (2003, background): “Structural and biochemical properties of end-joining proteins The KU heterodimer, consisting of a tight complex of KU70 (70 kDa) and KU80 (86 kDa), forms a closefitting asymmetrical ring that threads onto a free end of DNA as a nut on a bolt (Walker et al., 2001).”
DNA double-strand break repair: from mechanistic understanding to cancer treatment. (2007, background): “PK, which forms a ring that can specifically bind to DNA ends [11].”
Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. (2002, background): “In plants, the radiation occurred in intracellular proteins, whereas in nematodes and chordates there were Vol. 13, October 2002 3383 separate large expansions in the sets of extracellular, largely adhesive proteins, Third, if one considers the small set of VWA proteins common to all eukaryotes, the”