The results of computer modeling of plant kinesin-8/αβ-tubulin complexes with such αβ-tubulins' modified amino acid residues as phosphorylated Tyr262 and Tyr107 are reported in this paper. The molecular dynamics of these modified complexes in comparison with the dynamics of non-modified ones suggests that the phosphorylation of both α- and β-tubulins reveals stabilizing effect on the protein structure around the modified residue. It was found also that the phosphorylation of Tyr107 in β-tubulin molecule favors to more advantageous kinesin-8 binding with the phosphorylated microtubule surface in terms of energy.
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| http://dx.doi.org/10.1002/cbin.10818 | DOI Listing |
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3D-modeling of carboxyl-terminal phosphorylation of plant αβ-tubulin and its role in kinesin-8/microtubule interaction.
Cell Biol Int
September 2019
Department of Genomics and Molecular Biotechnology, Institute of Food Biotechnology and Genomics, Natl. Acad. Sci. of Ukraine, Osipovs'koho St., 2a, 04123, Kyiv, Ukraine.
The results of computer modeling of plant kinesin-8/αβ-tubulin complexes with such αβ-tubulins' modified amino acid residues as phosphorylated Tyr262 and Tyr107 are reported in this paper. The molecular dynamics of these modified complexes in comparison with the dynamics of non-modified ones suggests that the phosphorylation of both α- and β-tubulins reveals stabilizing effect on the protein structure around the modified residue. It was found also that the phosphorylation of Tyr107 in β-tubulin molecule favors to more advantageous kinesin-8 binding with the phosphorylated microtubule surface in terms of energy.
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