Abstract
ETS proteins are a family of widespread transcription factors that regulate the expression of many animal genes. Structurally, ETS proteins are characterized by a conserved DNA-binding ETS domain, which recognizes DNA sequences containing the trinucleotide GGA. The structural features of ETS domain-DNA complexes were analyzed, and conserved contacts important in terms of interaction stability and specificity were identified. The analysis revealed nine conserved hydrogen bonds with oxygens of DNA backbone phosphates, two bidentate hydrogen bonds with DNA major groove atoms, one conserved hydrophobic cluster located on the protein-DNA interface and important for binding site recognition, and 12 conserved water molecules presumably mediating the ETS domain-DNA interaction. The results are represented in specialized data bank of protein-DNA complexes (NPIDB).
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Original Russian Text © A.V. Grishin, A.V. Alexeevsky, S.A. Spirin, A.S. Karyagina, 2009, published in Molekulyarnaya Biologiya, 2009, Vol. 43, No. 4, pp. 666–674.
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Grishin, A.V., Alexeevsky, A.V., Spirin, S.A. et al. Conserved structural features of ETS domain-DNA complexes. Mol Biol 43, 612–619 (2009). https://doi.org/10.1134/S002689330904013X
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DOI: https://doi.org/10.1134/S002689330904013X