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PDBsum entry 6erh

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Top Page protein dna_rna ligands Protein-protein interface(s) links
DNA binding protein PDB id
6erh
Contents
Protein chains
490 a.a.
534 a.a.
DNA/RNA
Ligands
LYS-PRO-ARG-GLY-
LEU-PHE-SER
PRO-ARG-GLY-LEU-
PHE-SER
SO4 ×2
Waters ×33

References listed in PDB file
Key reference
Title Xlf and aplf bind ku80 at two remote sites to ensure DNA repair by non-Homologous end joining.
Authors C.Nemoz, V.Ropars, P.Frit, A.Gontier, P.Drevet, J.Yu, R.Guerois, A.Pitois, A.Comte, C.Delteil, N.Barboule, P.Legrand, S.Baconnais, Y.Yin, S.Tadi, E.Barbet-Massin, I.Berger, E.Le cam, M.Modesti, E.Rothenberg, P.Calsou, J.B.Charbonnier.
Ref. Nat Struct Mol Biol, 2018, 25, 971-980. [DOI no: 10.1038/s41594-018-0133-6]
PubMed id 30291363
Abstract
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 the NHEJ proteins APLF (A-KBM) and XLF (X-KBM) bound to a Ku-DNA complex. The two KBM motifs bind remote sites of the Ku80 α/β domain. The X-KBM occupies an internal pocket formed by an unprecedented large outward rotation of the Ku80 α/β domain. We observe independent recruitment of the APLF-interacting protein XRCC4 and of XLF to laser-irradiated sites via binding of A- and X-KBMs, respectively, to Ku80. Finally, we show that mutation of the X-KBM and A-KBM binding sites in Ku80 compromises both the efficiency and accuracy of end joining and cellular radiosensitivity. A- and X-KBMs may represent two initial anchor points to build the intricate interaction network required for NHEJ.
PROCHECK
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