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XRCC4 (X-ray cross-complementation group 4) and XLF (XRCC4-like factor) are two essential interacting proteins in the human NHEJ (non-homologous end-joining) pathway that repairs DNA DSBs (double-strand breaks). The individual crystal structures show that the dimeric proteins are homologues with protomers containing head domains and helical coiled-coil tails related by approximate two-fold symmetry. Biochemical, mutagenesis, biophysical and structural studies have identified the regions of interaction between the two proteins and suggested models for the XLF-XRCC4 complex. An 8.5 Å (1 Å = 0.1 nm) resolution crystal structure of XLF-XRCC4 solved by molecular replacement, together with gel filtration and nano-ESI (nano-electrospray ionization)-MS results, demonstrates that XLF and XRCC4 dimers interact through their head domains and form an alternating left-handed helical structure with polypeptide coiled coils and pseudo-dyads of individual XLF and XRCC4 dimers at right angles to the helical axis.

Original publication

DOI

10.1042/BST0391387

Type

Journal article

Journal

Biochem Soc Trans

Publication Date

10/2011

Volume

39

Pages

1387 - 1392

Keywords

Crystallization, DNA, DNA Breaks, Double-Stranded, DNA End-Joining Repair, DNA Ligases, DNA Repair, DNA Repair Enzymes, DNA-Binding Proteins, Dimerization, Humans, Models, Molecular, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary