Crystal structure of human XLF/Cernunnos reveals unexpected differences from XRCC4 with implications for NHEJ
نویسندگان
چکیده
منابع مشابه
Crystal structure of human XLF/Cernunnos reveals unexpected differences from XRCC4 with implications for NHEJ
The recently characterised 299-residue human XLF/Cernunnos protein plays a crucial role in DNA repair by non-homologous end joining (NHEJ) and interacts with the XRCC4-DNA Ligase IV complex. Here, we report the crystal structure of the XLF (1-233) homodimer at 2.3 A resolution, confirming the predicted structural similarity to XRCC4. The XLF coiled-coil, however, is shorter than that of XRCC4 a...
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XRCC4 is essential for carrying out non-homologous DNA end joining (NHEJ) in all eukaryotes and, in particular, V(D)J recombination in vertebrates. Xrcc4 protein forms a complex with DNA ligase IV that rejoins two DNA ends in the last step of V(D)J recombination and NHEJ to repair double strand breaks. XRCC4-defective cells are extremely sensitive to ionizing radiation, and disruption of the XR...
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ژورنال
عنوان ژورنال: The EMBO Journal
سال: 2007
ISSN: 0261-4189,1460-2075
DOI: 10.1038/sj.emboj.7601942