PTM对蛋白质主链构象影响的研究
Investigation of the impact of PTMs on the protein backbone conformation
摘要：
翻译后修饰（Post-translational Modifications，PTM）在蛋白质功能调控中起着重要作用。它们对蛋白质结构的影响以及它们与无序区域的联系在过去十年中已经被发现。尽管如此，由于翻译后修饰类型的高度多样性以及蛋白质修饰的多种方案（多个翻译后修饰、不同类型、不同时间等），使得翻译后修饰注释与蛋白质结构数据的直接对抗变得困难，因此我们分析了残基修饰对局部水平蛋白质结构的影响。由于有了一个专用的结构数据库，即PTM-SD，已经完成了一个大屏幕的PTM，并使用结构字母蛋白质块（PB）在局部蛋白质构象水平上进行分析。我们研究了PTM和修饰残基的骨架构象之间的关系，它们的局部环境，并在完整的蛋白质结构的水平。在非冗余数据集上研究了两种主要的PTM类型（N-糖基化和磷酸化），然后重点研究了4种不同的蛋白质，涵盖3种类型的PTM：肾素内肽酶和肝羧酸酯酶的N-糖基化，细胞周期蛋白依赖性激酶2（CDK 2）的磷酸化和肌动蛋白的甲基化。我们观察到，PTM可以稳定或不稳定的骨干结构，在本地和全球范围内，这些影响取决于PTM类型。
英文摘要：
Post-Translational Modifications (PTMs) are known to play a critical role in the regulation of the protein functions. Their impact on protein structures, and their link to disorder regions have already been spotted on the past decade. Nonetheless, the high diversity of PTMs types, and the multiple schemes of protein modifications (multiple PTMs, of different types, at different time, etc) make difficult the direct confrontation of PTM annotations and protein structures data.We so analyzed the impact of the residue modifications on the protein structures at local level. Thanks to a dedicated structure database, namely PTM-SD, a large screen of PTMs have been done and analyze at a local protein conformation levels using the structural alphabet Protein Blocks (PBs). We investigated the relation between PTMs and the backbone conformation of modified residues, of their local environment, and at the level of the complete protein structure. The two main PTM types (N-glycosylation and phosphorylation) have been studied in non-redundant datasets, and then, 4 different proteins were focused, covering 3 types of PTMs: N-glycosylation in renin endopeptidase and liver carboxylesterase, phosphorylation in cyclin-dependent kinase 2 (CDK2), and methylation in actin. We observed that PTMs could either stabilize or destabilize the backbone structure, at a local and global scale, and that these effects depend on the PTM types.
机构、总结、中文摘要均由AI分析而来，可能存在错误，请以论文正文为准。
