Protein–RNA interactions: Structural analysis and functional classes

• DOI: 10.1002/prot.21211
• Publication Date: 2006-12-21T22:17:21Z
• Authors: Jonathan J. Ellis; Mark Broom; Susan Jones
• Keywords: Models, Molecular; 0301 basic medicine; 570; Nucleotides; Amino Acid Motifs; Computational Biology; Proteins; Structural analysis; Hydrogen Bonding; 540; Protein Structure, Secondary; Protein Structure, Tertiary; Interaction propensity; 03 medical and health sciences; Protein-RNA interactions; Nucleic Acid Conformation; RNA; RNA binding proteins; Amino Acids; Nucleic Acid Recognition; Protein Binding

AbstractA data set of 89 protein–RNA complexes has been extracted from the Protein Data Bank, and the nucleic acid recognition sites characterized through direct contacts, accessible surface area, and secondary structure motifs. The differences between RNA recognition sites that bind to RNAs in functional classes has also been analyzed. Analysis of the complete data set revealed that van der Waals interactions are more numerous than hydrogen bonds and the contacts made to the nucleic acid backbone occur more frequently than specific contacts to nucleotide bases. Of the base‐specific contacts that were observed, contacts to guanine and adenine occurred most frequently. The most favored amino acid–nucleotide pairings observed were lysine–phosphate, tyrosine–uracil, arginine–phosphate, phenylalanine–adenine and tryptophan–guanine. The amino acid propensities showed that positively charged and polar residues were favored as expected, but also so were tryptophan and glycine. The propensities calculated for the functional classes showed trends similar to those observed for the complete data set. However, the analysis of hydrogen bond and van der Waal contacts showed that in general proteins complexed with messenger RNA, transfer RNA and viral RNA have more base specific contacts and less backbone contacts than expected, while proteins complexed with ribosomal RNA have less base‐specific contacts than the expected. Hence, whilst the types of amino acids involved in the interfaces are similar, the distribution of specific contacts is dependent upon the functional class of the RNA bound. Proteins 2007. © 2006 Wiley‐Liss, Inc.