Institute of Food Biotechnology and Genomics, Natl. Academy of Sci. of Ukraine, Osipovskogo str. 2a, Kyiv, 04123, Ukraine.
Cell Biol Int. 2019 Sep;43(9):1081-1090. doi: 10.1002/cbin.10810. Epub 2017 Aug 2.
According to the sequence and profile comparison with known catalytic domains, where identified protein phosphatases potentially involved in regulation of microtubule dynamics and structure from Arabidopsis thaliana, Nicotiana tabacum, Medicago sativa, Oryza sativa subsp. japonica, Zea mays, and Triticum aestivum. Selected proteins were related to classical non-receptor, serine/threonine-specific and dual protein phosphatases. By application of template structures of human protein phosphatases, it was performed homology modelling of the catalytic domains of 17 plant protein phosphatases. Based on the results of the structural alignment, molecular dynamics, and conservatism in positions of functionally importance, it was confirmed homology of selected plant proteins and known protein phosphatases regulating structure and dynamics of microtubules.
根据与已知催化结构域的序列和特征比较，鉴定出拟南芥、烟草、紫花苜蓿、水稻亚种粳稻、玉米和小麦中可能参与微管动力学和结构调节的蛋白磷酸酶。选定的蛋白质与经典的非受体、丝氨酸/苏氨酸特异性和双蛋白磷酸酶有关。通过应用人蛋白磷酸酶的模板结构，对 17 种植物蛋白磷酸酶的催化结构域进行了同源建模。基于结构比对、分子动力学和功能重要性位置保守性的结果，证实了所选植物蛋白与已知调节微管结构和动力学的蛋白磷酸酶的同源性。
