Molecular Biology

, Volume 43, Issue 4, pp 612–619

Conserved structural features of ETS domain-DNA complexes

  • A. V. Grishin
  • A. V. Alexeevsky
  • S. A. Spirin
  • A. S. Karyagina
Structural-Functional Analysis of Biopolymers and Their Complexes

DOI: 10.1134/S002689330904013X

Cite this article as:
Grishin, A.V., Alexeevsky, A.V., Spirin, S.A. et al. Mol Biol (2009) 43: 612. doi:10.1134/S002689330904013X

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).

Key words

ETS family protein-DNA interaction comparative analysis of related structures eukaryotic transcription factor 

Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • A. V. Grishin
    • 1
  • A. V. Alexeevsky
    • 2
    • 3
  • S. A. Spirin
    • 2
    • 3
  • A. S. Karyagina
    • 1
    • 4
  1. 1.All-Russia Institute of Agricultural BiotechnologyRussian Academy of Agricultural SciencesMoscowRussia
  2. 2.Belozersky Institute of Physico-Chemical BiologyMoscow State UniversityMoscowRussia
  3. 3.Institute of System StudiesRussian Academy of SciencesMoscowRussia
  4. 4.Gamaleya Institute of Epidemiology and MicrobiologyRussian Academy of Medical SciencesMoscowRussia

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