Protein-RNA Interactions: structural analysis and functional classes

Ellis, Jonathan J, Broom, Mark and Jones, Susan (2007) Protein-RNA Interactions: structural analysis and functional classes. Proteins, 66 (4). pp. 903-911. ISSN 0887-3585

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Abstract

A 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.

Item Type: Article
Additional Information: SJ directed the research and was the corresponding author
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Jonathan Ellis
Date Deposited: 06 Feb 2012 19:36
Last Modified: 24 May 2012 13:27
URI: http://sro.sussex.ac.uk/id/eprint/21468
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