<p> This domain is found in a number of transcription factors, including p53, NFATC, TonEBP, STAT-1, and NFkappaB, where it is responsible for DNA-binding. These transcription factors play diverse roles in the regulation of cellular functions: the p53 tumour suppressor upregulates the expression of genes involved in cell cycle arrest and apoptosis [<cite idref="PUB00011797"/>]; NFATC regulates the production of effector proteins involved in coordinating the immune response [<cite idref="PUB00011799"/>]; TonEBP regulates gene expression induced by osmotic stress and helps regulate intracellular volume during cell growth [<cite idref="PUB00011802"/>]; STAT-1 plays an important role in B lymphocyte growth and function [<cite idref="PUB00011801"/>]; and NFkappaB is involved in the inflammatory response [<cite idref="PUB00011803"/>]. The DNA-binding domain acts to clamp, or in the case of TonEBP, encircle the DNA target in order to stabilise the protein-DNA complex [<cite idref="PUB00011800"/>]. Protein interactions may also serve to stabilise the protein-DNA complex, for example in the STAT-1 dimer the SH2 (Src homology 2) domain in each monomer is coupled to the DNA-binding domain to increase stability [<cite idref="PUB00011807"/>]. The DNA-binding domain consists of a beta-sandwich formed of 9 strands in 2 sheets with a Greek-key topology. This structure is found in many transcription factors, often within the DNA-binding domain.</p> p53-like transcription factor, DNA-binding