Computational methods for prediction of protein-RNA interactions

被引:71
|
作者
Puton, Tomasz [2 ]
Kozlowski, Lukasz [1 ]
Tuszynska, Irina [1 ]
Rother, Kristian [2 ]
Bujnicki, Janusz M. [1 ,2 ]
机构
[1] Int Inst Mol & Cell Biol, Lab Bioinformat & Prot Engn, PL-02109 Warsaw, Poland
[2] Adam Mickiewicz Univ, Fac Biol, Inst Mol Biol & Biotechnol, Bioinformat Lab, PL-61614 Poznan, Poland
基金
欧洲研究理事会;
关键词
RNA; Protein; RNP; Binding site prediction; Macromolecular docking; Structural bioinformatics; BINDING-SITES; EVOLUTIONARY INFORMATION; STRUCTURAL-ANALYSIS; DOCKING; RECOGNITION; SERVER; DNA; COMPLEXES; SEQUENCES; RESIDUES;
D O I
10.1016/j.jsb.2011.10.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Understanding the molecular mechanism of protein-RNA recognition and complex formation is a major challenge in structural biology. Unfortunately, the experimental determination of protein-RNA complexes by X-ray crystallography and nuclear magnetic resonance spectroscopy (NMR) is tedious and difficult. Alternatively, protein-RNA interactions can be predicted by computational methods. Although less accurate than experimental observations, computational predictions can be sufficiently accurate to prompt functional hypotheses and guide experiments, e.g. to identify individual amino acid or nucleotide residues. In this article we review 10 methods for predicting protein-RNA interactions, seven of which predict RNA-binding sites from protein sequences and three from structures. We also developed a meta-predictor that uses the output of top three sequence-based primary predictors to calculate a consensus prediction, which outperforms all the primary predictors. In order to fully cover the software for predicting protein-RNA interactions, we also describe five methods for protein-RNA docking. The article highlights the strengths and shortcomings of existing methods for the prediction of protein-RNA interactions and provides suggestions for their further development. (C) 2011 Esevier Inc. All rights reserved.
引用
收藏
页码:261 / 268
页数:8
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