Evaluating conformational changes in protein structures binding RNA

Ellis, Jonathan J and Jones, Susan (2008) Evaluating conformational changes in protein structures binding RNA. Proteins, 70 (4). pp. 1518-1526. ISSN 0887-3585

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Many protein-RNA recognition events are known to exhibit conformational changes from qualitative observations of individual complexes. However, a quantitative estimation of conformational changes is required if protein-RNA docking and template-based methods for RNA binding site prediction are to be developed. This study presents the first quantitive evaluation of conformational changes that occur when proteins bind RNA. The analysis of twelve RNA-binding proteins in the bound and unbound states using error-scaled difference distance matrices is presented. The binding site residues are mapped to each structure, and the conformational changes that affect these residues are evaluated. Of the twelve proteins four exhibit greater movements in nonbinding site residues, and a further four show the greatest movements in binding site residues. The remaining four proteins display no significant conformational change. When interface residues are found to be in conformationally variable regions of the protein they are typically seen to move less than 2 Å between the bound and unbound conformations. The current data indicate that conformational changes in the binding site residues of RNA binding proteins may not be as significant as previously suggested, but a larger data set is required before wider conclusions may be drawn. The implications of the observed conformational changes for protein function prediction are discussed.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Jonathan Ellis
Date Deposited: 06 Feb 2012 18:40
Last Modified: 24 May 2012 13:29
URI: http://sro.sussex.ac.uk/id/eprint/17668
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