MTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest H-1117, Hungary.
Nucleic Acids Res. 2018 Jul 2;46(W1):W329-W337. doi: 10.1093/nar/gky384.
The structural states of proteins include ordered globular domains as well as intrinsically disordered protein regions that exist as highly flexible conformational ensembles in isolation. Various computational tools have been developed to discriminate ordered and disordered segments based on the amino acid sequence. However, properties of IDRs can also depend on various conditions, including binding to globular protein partners or environmental factors, such as redox potential. These cases provide further challenges for the computational characterization of disordered segments. In this work we present IUPred2A, a combined web interface that allows to generate energy estimation based predictions for ordered and disordered residues by IUPred2 and for disordered binding regions by ANCHOR2. The updated web server retains the robustness of the original programs but offers several new features. While only minor bug fixes are implemented for IUPred, the next version of ANCHOR is significantly improved through a new architecture and parameters optimized on novel datasets. In addition, redox-sensitive regions can also be highlighted through a novel experimental feature. The web server offers graphical and text outputs, a RESTful interface, access to software download and extensive help, and can be accessed at a new location: http://iupred2a.elte.hu.
蛋白质的结构状态包括有序的球状结构域以及作为高度灵活的构象集合存在的固有无序蛋白质区域。已经开发了各种计算工具来根据氨基酸序列区分有序和无序片段。然而，IDR 的特性也可能取决于各种条件，包括与球状蛋白伴侣的结合或环境因素，如氧化还原电位。这些情况为无序片段的计算特征提供了进一步的挑战。在这项工作中，我们展示了 IUPred2A，这是一个组合的网络界面，允许通过 IUPred2 对有序和无序残基以及通过 ANCHOR2 对无序结合区域生成基于能量估计的预测。更新后的网络服务器保留了原始程序的稳健性，但提供了几个新功能。虽然仅对 IUPred 进行了小的错误修复，但通过新的架构和针对新数据集优化的参数，对 ANCHOR 的下一个版本进行了显著改进。此外，还可以通过新的实验功能突出显示氧化还原敏感区域。该网络服务器提供图形和文本输出、RESTful 接口、软件下载访问和广泛的帮助，并可在新位置访问：http://iupred2a.elte.hu。
