Abstract
ETS proteins comprise a family of widespread transcription factors regulating expression of many animal genes. Structurally ETS proteins are characterized by conserved DNA-binding ETS domain, recognizing DNA sequences with trinucleotide GGA. Comparative analysis of structural features of ETS domain-DNA complexes was carried out and conserved contacts, important in terms of interaction stability and specificity were identified. The analysis revealed 9 conserved hydrogen bonds with DNA backbone phosphates and 2 conserved bidentate hydrogen bonds with DNA major groove atoms, one conserved hydrophobic cluster on protein-DNA interface, important for binding site recognition, and 12 conserved water molecules, possibly mediating ETS domain-DNA interaction. The results are represented in specialized data bank of protein-DNA complexes NPIDB.
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