XLF and APLF bind Ku80 at two remote sites to ensure DNA repair by non-homologous end joining

The Ku70-Ku80 (Ku) heterodimer binds rapidly and tightly to the ends of DNA double-strand breaks and recruits factors of the non-homologous end-joining (NHEJ) repair pathway through molecular interactions that remain unclear. We have determined crystal structures of the Ku-binding motifs (KBM) of th...

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Vydáno v:	Nature structural & molecular biology Ročník 25; číslo 10; s. 971 - 980
Hlavní autoři:	Nemoz, Clement, Ropars, Virginie, Frit, Philippe, Gontier, Amandine, Drevet, Pascal, Yu, Jinchao, Guerois, Raphaël, Pitois, Aurelien, Comte, Audrey, Delteil, Christine, Barboule, Nadia, Legrand, Pierre, Baconnais, Sonia, Yin, Yandong, Tadi, Satish, Barbet-Massin, Emeline, Berger, Imre, Le Cam, Eric, Modesti, Mauro, Rothenberg, Eli, Calsou, Patrick, Charbonnier, Jean Baptiste
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Nature Publishing Group 01.10.2018
Témata:	Binding sites Conserved Sequence Crystal structure Crystallography, X-Ray Deoxyribonucleic acid DNA DNA damage DNA End-Joining Repair DNA repair DNA Repair Enzymes - chemistry DNA Repair Enzymes - metabolism DNA Repair Enzymes - physiology DNA-(Apurinic or Apyrimidinic Site) Lyase - chemistry DNA-(Apurinic or Apyrimidinic Site) Lyase - metabolism DNA-(Apurinic or Apyrimidinic Site) Lyase - physiology DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology Homology Humans Ku Autoantigen - chemistry Ku Autoantigen - metabolism Ku Autoantigen - physiology Models, Molecular Molecular interactions Mutation Non-homologous end joining Poly-ADP-Ribose Binding Proteins - chemistry Poly-ADP-Ribose Binding Proteins - metabolism Poly-ADP-Ribose Binding Proteins - physiology Protein Domains Proteins Radiosensitivity Repair
ISSN:	1545-9993, 1545-9985, 1545-9985
On-line přístup:	Získat plný text
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