Reconstruction of spatial structure of plant protein phosphatase type 1, 2а and 4 in complexes with microcystin-LR

  • D. A. Samofalova Institute of Food Biotechnology and Genomics, Natl. Academy of Sci. of Ukraine, Ukraine, 04123, Kyiv, Osipovskogo str., 2a
  • P. A. Karpov Institute of Food Biotechnology and Genomics, Natl. Academy of Sci. of Ukraine, Ukraine, 04123, Kyiv, Osipovskogo str., 2a
  • O. V. Raievskyi Institute of Food Biotechnology and Genomics, Natl. Academy of Sci. of Ukraine, Ukraine, 04123, Kyiv, Osipovskogo str., 2a
  • Ya. B. Blume Institute of Food Biotechnology and Genomics, Natl. Academy of Sci. of Ukraine, Ukraine, 04123, Kyiv, Osipovskogo str., 2a
DOI: https://doi.org/10.7124/FEEO.v20.791

Abstract

Aim. The major toxicity of Microcystin-LR (MCLR) has been ascribed to its potent ability to inhibit serine/threonine-specific protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A). Although MCLR is widely used in animal models its selectivity for these enzymes of plant origin is not still investigated in details for phylogenetically diversified sources. Methods. The spatial structure of plant PP1, PP2A, PP4 protein phosphatases was reconstructed with homology modeling method. Flexible docking of MCLR was performed using CCDC GOLD Suite 5.3. For docking evaluations, GOLD scoring functions were used. Results. Information about amino acids, involved in ligand binding, was obtained from 8 experimentally proved human MCLR-PP1 and PP2A complexes. The sites of microcystin-LR binding with plant protein phosphatases (type-1, 2А and 4) were proved by comparative analysis and molecular docking. A high level of sequence and structure identity of plant and animal phosphatases allow us to conclude similarity of MCLR binding in PP1, PP2A and PP4.

Keywords: microcystin-LR, protein phosphatase, specific interaction, molecular docking.

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