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Identification of Protein-RNA Interaction Sites Using the Information of Spatial Adjacent Residues

Overview
Journal Proteome Sci
Publisher Biomed Central
Date 2011 Dec 15
PMID 22165911
Citations 3
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Abstract

Background: Protein-RNA interactions play an important role in numbers of fundamental cellular processes such as RNA splicing, transport and translation, protein synthesis and certain RNA-mediated enzymatic processes. The more knowledge of Protein-RNA recognition can not only help to understand the regulatory mechanism, the site-directed mutagenesis and regulation of RNA-protein complexes in biological systems, but also have a vitally effecting for rational drug design.

Results: Based on the information of spatial adjacent residues, novel feature extraction methods were proposed to predict protein-RNA interaction sites with SVM-KNN classifier. The total accuracies of spatial adjacent residue profile feature and spatial adjacent residues weighted accessibility solvent area feature are 78%, 67.07% respectively in 5-fold cross-validation test, which are 1.4%, 3.79% higher than that of sequence neighbour residue profile feature and sequence neighbour residue accessibility solvent area feature.

Conclusions: The results indicate that the performance of feature extraction method using the spatial adjacent information is superior to the sequence neighbour information approach. The performance of SVM-KNN classifier is little better than that of SVM. The feature extraction method of spatial adjacent information with SVM-KNN is very effective for identifying protein-RNA interaction sites and may at least play a complimentary role to the existing methods.

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Protein-RNA interface residue prediction using machine learning: an assessment of the state of the art.

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References
1.
Henikoff S, Henikoff J . Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A. 1992; 89(22):10915-9. PMC: 50453. DOI: 10.1073/pnas.89.22.10915. View

2.
Jeong E, Chung I, Miyano S . A neural network method for identification of RNA-interacting residues in protein. Genome Inform. 2005; 15(1):105-16. View

3.
Ecker , Griffey . RNA as a small-molecule drug target: doubling the value of genomics. Drug Discov Today. 1999; 4(9):420-429. DOI: 10.1016/s1359-6446(99)01389-6. View

4.
Wang Y, Xue Z, Shen G, Xu J . PRINTR: prediction of RNA binding sites in proteins using SVM and profiles. Amino Acids. 2008; 35(2):295-302. DOI: 10.1007/s00726-007-0634-9. View

5.
Terribilini M, Lee J, Yan C, Jernigan R, Honavar V, Dobbs D . Prediction of RNA binding sites in proteins from amino acid sequence. RNA. 2006; 12(8):1450-62. PMC: 1524891. DOI: 10.1261/rna.2197306. View