[5][6][7] Nibrin is a protein associated with the repair of double strand breaks (DSBs) which pose serious damage to a genome.

It is a 754 amino acid protein identified as a member of the NBS1/hMre11/RAD50(N/M/R, more commonly referred to as MRN) double strand DNA break repair complex.

[8] This complex recognizes DNA damage and rapidly relocates to DSB sites and forms nuclear foci.

It also has a role in regulation of N/M/R (MRN) protein complex activity which includes end-processing of both physiological and mutagenic DNA double strand breaks (DSBs).

[9] Cellular response is performed by damage sensors, effectors of lesion repair and signal transduction.

The central role is carried out by ataxia telangiectasia mutated (ATM) by activating the DSB signaling cascade, phosphorylating downstream substrates such as histone H2AX and NBS1.

[12] These individuals appear to be primarily defective in homologous recombination, a process that accurately repairs double-strand breaks, both in somatic cells and during meiosis.

However, NBS1 mediated MMEJ repair is highly inaccurate, so in this case, over-expression, rather than under-expression, apparently leads to cancer.

This suggests that in general, viruses commonly interact in intrinsically disordered domains in host proteins.

The evolution of increased disorder in nibrin benefits the host in decreasing ICP0 interaction and virus hijack.

It has been shown in studies that activation of the MRN complex and ATM biochemical cascade is consistent for a resulting HSV-1 infection.