Amino acid residue doublet propensity in the protein–RNA interface and its application to RNA interface prediction
| Autor: | Oanh T. P. Kim, Kei Yura, Nobuhiro Go |
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| Rok vydání: | 2006 |
| Předmět: |
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Molecular Nucleocytoplasmic Transport Proteins Stereochemistry RNA-binding protein Biology DEAD-box RNA Helicases Gene expression Genetics Humans RNA Messenger Amino Acids Binding site Databases Protein Messenger RNA Residue (complex analysis) Binding Sites Computational Biology RNA-Binding Proteins RNA computer.file_format Protein Data Bank Biochemistry Data Interpretation Statistical RNA splicing computer Protein Binding |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkl819 |
| Popis: | Protein–RNA interactions play essential roles in a number of regulatory mechanisms for gene expression such as RNA splicing, transport, translation and post-transcriptional control. As the number of available protein–RNA complex 3D structures has increased, it is now possible to statistically examine protein–RNA interactions based on 3D structures. We performed computational analyses of 86 representative protein–RNA complexes retrieved from the Protein Data Bank. Interface residue propensity, a measure of the relative importance of different amino acid residues in the RNA interface, was calculated for each amino acid residue type (residue singlet interface propensity). In addition to the residue singlet propensity, we introduce a new residue-based propensity, which gives a measure of residue pairing preferences in the RNA interface of a protein (residue doublet interface propensity). The residue doublet interface propensity contains much more information than the sum of two singlet propensities alone. The prediction of the RNA interface using the two types of propensities plus a position-specific multiple sequence profile can achieve a specificity of about 80%. The prediction method was then applied to the 3D structure of two mRNA export factors, TAP (Mex67) and UAP56 (Sub2). The prediction enables us to point out candidate RNA interfaces, part of which are consistent with previous experimental studies and may contribute to elucidation of atomic mechanisms of mRNA export. |
| Databáze: | OpenAIRE |
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