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NeProc可预测内在无序区域中的结合片段,而无需学习结合区域序列。

NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences.

作者信息

Anbo Hiroto, Amagai Hiroki, Fukuchi Satoshi

机构信息

Department of Life Science and Informatics, Faculty of Engineering, Maebashi Institute of Technology, Maebashi, Gunma 371-0816, Japan.

出版信息

Biophys Physicobiol. 2020 Nov 3;17:147-154. doi: 10.2142/biophysico.BSJ-2020026. eCollection 2020.

DOI:10.2142/biophysico.BSJ-2020026
PMID:33304713
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7692026/
Abstract

Intrinsically disordered proteins are those proteins with intrinsically disordered regions. One of the unique characteristics of intrinsically disordered proteins is the existence of functional segments in intrinsically dis-ordered regions. These segments are involved in binding to partner molecules, such as protein and DNA, and play important roles in signaling pathways and/or transcriptional regulation. Although there are databases that gather information on such disordered binding regions, data remain limited. Therefore, it is desirable to develop programs to predict the disordered binding regions without using data for the binding regions. We developed a program, NeProc, to predict the disordered binding regions, which can be regarded as intrinsically disordered regions with a structural propensity. We only used data for the structural domains and intrinsically disordered regions to detect such regions. NeProc accepts a query amino acid sequence converted into a position specific score matrix, and uses two neural networks that employ different window sizes, a neural network of short windows, and a neural network of long windows. The performance of NeProc was comparable to that of existing programs of the disordered binding region prediction. This result presents the possibility to overcome the shortage of the disordered binding region data in the development of the prediction programs for these binding regions. NeProc is available at http://flab.neproc.org/neproc/index.html.

摘要

内在无序蛋白质是指那些具有内在无序区域的蛋白质。内在无序蛋白质的独特特征之一是在内在无序区域存在功能片段。这些片段参与与伴侣分子(如蛋白质和DNA)的结合,并在信号通路和/或转录调控中发挥重要作用。尽管有数据库收集关于此类无序结合区域的信息,但数据仍然有限。因此,期望开发不使用结合区域数据来预测无序结合区域的程序。我们开发了一个名为NeProc的程序来预测无序结合区域,该区域可被视为具有结构倾向的内在无序区域。我们仅使用结构域和内在无序区域的数据来检测此类区域。NeProc接受转换为位置特异性评分矩阵的查询氨基酸序列,并使用两个采用不同窗口大小的神经网络,即短窗口神经网络和长窗口神经网络。NeProc的性能与现有的无序结合区域预测程序相当。这一结果表明在开发这些结合区域的预测程序时有可能克服无序结合区域数据不足的问题。NeProc可在http://flab.neproc.org/neproc/index.html上获取。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/ee72ad49d6ac/17_147-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/d5bd4c190c2e/17_147-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/4794506ce616/17_147-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/ee72ad49d6ac/17_147-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/d5bd4c190c2e/17_147-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/4794506ce616/17_147-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05cb/7692026/ee72ad49d6ac/17_147-g003.jpg

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本文引用的文献

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DisProt: intrinsic protein disorder annotation in 2020.DisProt:2020 年的内在蛋白无序注释。
Nucleic Acids Res. 2020 Jan 8;48(D1):D269-D276. doi: 10.1093/nar/gkz975.
2
Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins.疾病相关蛋白中无规则区域的功能片段。
Biomolecules. 2019 Mar 5;9(3):88. doi: 10.3390/biom9030088.
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IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding.IUPred2A:氧化还原状态和蛋白质结合依赖性的蛋白质无序性预测的上下文相关分析。
Nucleic Acids Res. 2018 Jul 2;46(W1):W329-W337. doi: 10.1093/nar/gky384.
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Sequence conservation of protein binding segments in intrinsically disordered regions.内在无序区域中蛋白质结合片段的序列保守性。
Biochem Biophys Res Commun. 2017 Dec 16;494(3-4):602-607. doi: 10.1016/j.bbrc.2017.10.099. Epub 2017 Oct 21.
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MobiDB-lite: fast and highly specific consensus prediction of intrinsic disorder in proteins.MobiDB-lite:蛋白质内在无序的快速且高度特异的一致性预测
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