 |
PDBsum entry 6erh
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
6erh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
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: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |