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Updated: Mar 22, 2026

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
Published on: February 7, 2019
Conserved features of complexes of TATA-box binding proteins with DNA
Olga Zanegina1, Evgeniy Aksianov1, Andrei V Alexeevski1,2
1* Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 1 Leninskiye Gory, bld.40, Moscow 119991, Russia.
Abstract:
A comparative analysis of all available structures of complexes of TATA-box binding proteins (TBPs) with DNA is performed. Conserved features of DNA-protein interaction are described, including nine amino acid residues that form conserved hydrogen bonds, 13 residues participating in formation of two conserved hydrophobic clusters at DNA-protein interface, and four conserved water-mediated contacts. Partial symmetry of conserved contacts reflects quasi-symmetry of TBP structure.
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