4.4 Article

Non-homologous end-joining partners in a helical dance: structural studies of XLF-XRCC4 interactions

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 39, 期 -, 页码 1387-1392

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BST0391387

关键词

double-strand break (DSB); non-homologous end-joining (NHEJ); X-ray cross-complementation group 4 (XRCC4); XRCC4-like factor (XLF)

资金

  1. Wellcome Trust

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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 angstrom (1 angstrom = 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.

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