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Structural-biological characteristics of tubulin interaction with dinitoanilines
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The interaction of dinitroaniline compounds with tubulin molecules is characterized by extraordinary selectivity – these matters effectively associate with plant as well as protozoan tubulin and practically don’t interact with fungal and animal tubulin in spite of extraordinarily high level of similarity of their sequences. Structural features and mechanisms of this interaction are generalized and in detail analysed in this research. In particular, the regularities of dinitroaniline binding sites’ structure and localization on surfaces of tubulin different subunits and tubulins of different origin are characterized. Dinitroaniline binding sites are disposed on the surfaces of longitudinal contacts between tubulin subunits, contain residues of diamine amino acids (lysine or arginine) coupling al nitrile group (s) of dinitroanilines. Binding site location on the surfaces of the same subunit of different origin (for example, plant and protozoan a-tubulins) is coincided, however site localisation on surface of a- and b-subunits is distinct. The described sites potentially can be the binding areas for another antimicrotubular compounds, in particular, cyanoacrilates.
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|Coded & Designed by Volodymyr Duplij||Modified 25.07.21|