Majila Kartik, Viswanath Shruthi
National Center for Biological Sciences, Tata Institute of Fundamental Research, Bangalore, India 560065.
bioRxiv. 2024 Aug 26:2024.08.22.609111. doi: 10.1101/2024.08.22.609111.
Intrinsically disordered regions (IDRs) of proteins exist as an ensemble of conformations, and not as a single structure. Existing databases contain extensive, experimentally derived annotations of intrinsic disorder for millions of proteins at the sequence level. However, only a tiny fraction of these IDRs are associated with an experimentally determined protein structure. Moreover, even if a structure exists, parts of the disordered regions may still be unresolved.
Here we organize uctures of ntrinsically isordered egions (StrIDR), a database of IDRs confirmed experimental or homology-based evidence, resolved in experimentally determined structures. The database can provide useful insights into the dynamics, folding, and interactions of IDRs. It can also facilitate computational studies on IDRs, such as those using molecular dynamics simulations and/or machine learning.
StrIDR is available at https://isblab.ncbs.res.in/stridr. The web UI allows for downloading PDB structures and SIFTS mappings of individual entries. Additionally, the entire database can be downloaded in a JSON format. The source code for creating and updating the database is available at https://github.com/isblab/stridr.
蛋白质的内在无序区域(IDR)以构象集合的形式存在,而非单一结构。现有数据库包含数百万种蛋白质在序列水平上广泛的、通过实验得出的内在无序注释。然而,这些IDR中只有极小一部分与通过实验确定的蛋白质结构相关。此外,即使存在结构,无序区域的部分可能仍然无法解析。
在此,我们整理了内在无序区域结构数据库(StrIDR),该数据库包含基于实验或同源性证据确认的、在实验确定的结构中解析出的IDR。该数据库可为IDR的动力学、折叠和相互作用提供有用的见解。它还可以促进对IDR的计算研究,例如使用分子动力学模拟和/或机器学习的研究。