Revealing molecular mechanisms of sequence-specific recognition of DNA by proteins is one of the key tasks of biology. The current review presents the results of statistical analysis of the structural databases obtained by different scientific groups studying the conformational features of free and protein-bound DNA fragments that could be used for clarifying the mechanisms of protein-nucleic acid recognition. The analysis of the published data allowed us to make the following generalizations. The ability of DNA double helix to adopt alternative conformations, including the ones of sugarphosphate backbone, is an intrinsic characteristic of certain DNA sequences. Such conformational transitions are the potential sources of formation of unique geometry of the dinucleotide steps and/or individual nucleotides and lead to alteration of base stacking and/or changes of the assessable surface area of atoms, and can be the criteria of recognition of DNA by protein as well. Changes in the physical properties that depend on the DNA structure, i. e. the polar/unpolar profile and electrostatic potential of the grooves, can also be used by protein for DNA readout

The article describes a new database (ProtNA-ASA), which combines the data on conformational parameters of nucleic acids and calculations of the accessible surface area (ASA) of nucleic acid atoms in protein-DNA/RNA complexes. As for October 2008, the database contains 214 DNA-protein and 28 RNA-protein nonhomologous complexes. The database provides structural parameters that describe local geometry of base pairs and base-pair steps as well as backbone torsion angles. Additionally, total ASA of DNA/RNA atoms and the accessible area of atoms in the minor and major grooves are calculated. ProtNA-ASA database facilitates studying the relationship between the DNA/RNA conformation and availability of atoms for contact with proteins either in major or in minor groove for different nucleotides. Such an analysis is important for understanding the principles of molecular recognition including indirect sequence readout. The database is publicly available for use at

Protein-nucleic acid recognition is essential in a number of cellular processes, in particular, gene regulation, DNA replication and compaction. Studies on the recognition mechanisms show that DNA sequence carries information which is read out by proteins that selectively bind to specific DNA sites. The review is focused on the processes taking place during formation of specific and nonspecific complexes of proteins and DNA. Special attention is paid to direct and indirect mechanisms of sequence-specific recognition. Several examples of protein-nucleic acid complexes are given to illustrate the variety of recognition mechanism

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