2026年的DisProt:增强内在无序蛋白质的可访问性,沉积和注释
Maria Victoria Nugnes1, Kamel Eddine Adel Bouhraoua1, Mehdi Zoubiri1
1Department of Biomedical Sciences, University of Padova, Padova 35131, Italy.
Nucleic acids research
|November 18, 2025
概括
对于内在无序蛋白质 (IDP) 的数据库DisProt已经扩展了其证据和特征. 它现在集成了计算预测,并提高了研究蛋白质疾病的研究人员的数据可访问性.
科学领域:
- 生物化学 生物化学
- 生物信息学是一种生物信息学.
- 结构生物学 结构生物学
背景情况:
- 内在无序的蛋白质 (IDP) 和区域 (IDR) 缺乏稳定的3D结构,在细胞功能中发挥关键作用.
- 像DisProt这样的数据库对于策划和传播关于IDP和IDR的实验证据至关重要.
- 越来越多的IDP研究需要在数据管理和可访问性方面不断更新和改进.
研究的目的:
- 介绍DisProt数据库的最新版本,强调其增长和新功能.
- 改进实验数据的整合和可访问性 关于内在无序的蛋白质和区域.
- 通过新的功能和数据扩展,增强DisProt对研究人员的实用性.
主要方法:
- 系统地采用关于疾病实验的最低信息 (MIADE) 准则,用于详细的注释.
- 扩展DisProt数据通过基于BLAST的同类传播在MobiDB.
- 将计算预测作为有效证据与实验数据相结合.
- 内在无序蛋白质 (IDP) 实体学的更新和重组.
主要成果:
- 现在DisProt包含3201个IDP和13,347个证据,超过1500个新的结构状态和1300个新的功能注释.
- 通过MIADE,试验细节的注释量增加了一倍以上,从而提高了可解释性.
- 障碍区域和相互作用已经通过同质传播扩展到数十万种蛋白质.
- 该数据库现在集成了计算预测,并提供了更新的IDP Ontology,以提高准确性和互操作性.
结论:
- 增强的DisProt数据库为研究内在无序蛋白质提供了更全面和更容易获得的资源.
- 新功能,包括集成的计算预测和更新的本体学,提高数据准确性和语义清晰度.
- 迪斯普罗特的演变成为混合知识库和存储系统,以及社区参与工具,支持更广泛的研究参与.
更多相关视频
07:24Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
2.2K
05:13Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
Published on: January 12, 2024
1.4K
相关概念视频
02:18Intrinsically Disordered Proteins
19.2K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.2K
02:18Intrinsically Disordered Proteins
2.7K
2.7K
01:24Protein Organization
9.0K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
9.0K
02:04Protein-protein Interfaces
14.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.4K