DNA ligase

DNA ligase IV (EC 6.5.1.1), which is conserved in all eukaryotes, is part of a family of ATP-dependent DNA ligases that are involved in DNA replication, recombination and repair. It is a nuclear enzyme that joins the breaks in the phosphodiester backbone of DNA by the process of non-homologous end joining (NHEJ)[1]. DNA ligases have two common domains:  a catalytic domain (CD) that contains several conserved nucleotide-binding motifs, and a conserved non-catalytic domain (NCD).  In addition, DNA ligase IV has a long C-terminal extension comprising of two BRCT domains (after the C-terminal domain of a breast cancer susceptibility protein, BRCA1), which are phosphopeptide-binding modules found in many proteins that regulate DNA damage responses (such as BRCA1, MDC1 and BARD1). These BRCT domains are connected to a short linker region that is required for the binding of the XRCC4 protein, which is important for ligase activity[2].


[1] IV Martin et al. ATP-dependent DNA ligases. Genome Biol. 2002;3(4):REVIEWS3005. Epub 2002 Mar 19.
[2] T Ellenberger et al. Eukaryotic DNA ligases: structural and functional insights. Annu Rev Biochem. 2008;77:313-38.

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Axon ID Name Description From price
2531 SCR7 pyrazine DNA ligase IV mediated inhibitor of NHEJ €65.00
2549 L67 Cytotoxic inhibitor of DNA ligase I and III €90.00

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