Amino acid residue doublet propensity in the protein-RNA interface and its application to RNA interface prediction

Oanh T.P. Kim, Kei Yura*, Nobuhiro Go

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

100 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)6450-6460
Number of pages11
JournalNucleic acids research
Issue number22
Publication statusPublished - 2006 Dec
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


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