Open AccessReconstruction of spatial structure of plant protein phosphatase type 1, 2a and 4 in complexes with microcystin-LR
Author(s) -
Dariia Samofalova,
П. А. Карпов,
O. V. Raievskyi,
Ya. B. Blume
Publication year - 1970
Publication title -
faktori eksperimentalʹnoï evolûcìï organìzmìv
Language(s) - English
Resource type - Journals
eISSN - 2415-3826
pISSN - 2219-3782
DOI - 10.7124/feeo.v20.791
Subject(s) - protein phosphatase 2 , phosphatase , serine , docking (animal) , homology modeling , microcystin , microcystin lr , threonine , biochemistry , biology , binding site , chemistry , phosphorylation , enzyme , genetics , cyanobacteria , medicine , nursing , bacteria
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, 2A 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.