Abstract

Eighteen isotypes of CK1-like protein kinases were identified in A. thaliana. Comparison of catalytic domains in rat CK1 (α, β, γ1–3, δ, and ε) and 18 plant homologs from A. thaliana confirmed a high structural similarity for 13 CK1-like protein kinases: CKL1 (CK1δ), CKL2, CKL3, CKL4, CKL5, CKL6, CKL7, CKL8, CKL9, CKL10, CKL11, CKL12, and CKL13. It was found that CK1-specific inhibitor D4476 interacts with rat KС1D and 13 plant homologs in a similar ATP-competitive manner. Ligand binding was confirmed based on scoring functions of docking, results of molecular dynamics, and chemogenomic analysis. The specific interaction of CK1-kinases with substrate proteins depends on specific motifs located in their C-end region. The specific motifs of EB1 binding was identified in plant СKL1 and CKL2. The role of the C-end region in CKL6–β-tubulin interaction was also confirmed.

中文翻译：

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CK1样蛋白激酶同工型与植物微管调控相关的结构生物学特性

摘要

在拟南芥中鉴定出十八种同型的CK1样蛋白激酶。大鼠CK1（α，β，γ1-3，δ和ε）中的催化结构域与拟南芥中18种植物同源物的比较证实了13种CK1样蛋白激酶的高度结构相似性：CKL1（CK1δ），CKL2，CKL3，CKL4，CKL5，CKL6，CKL7，CKL8，CKL9，CKL10，CKL11，CKL12和CKL13。发现CK1特异性抑制剂D4476以相似的ATP竞争方式与大鼠KС1D和13种植物同源物相互作用。基于对接的评分功能，分子动力学结果和化学基因组分析，确定了配体结合。CK1激酶与底物蛋白的特异性相互作用取决于位于其C端区域的特定基序。在植物СKL1和CKL2中鉴定了EB1结合的特定基序。还确认了C末端区域在CKL6-β-微管蛋白相互作用中的作用。