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RNA-binding residues prediction using structural features.


ABSTRACT: RNA-protein complexes play an essential role in many biological processes. To explore potential functions of RNA-protein complexes, it's important to identify RNA-binding residues in proteins.In this work, we propose a set of new structural features for RNA-binding residue prediction. A set of template patches are first extracted from RNA-binding interfaces. To construct structural features for a residue, we compare its surrounding patches with each template patch and use the accumulated distances as its structural features. These new features provide sufficient structural information of surrounding surface of a residue and they can be used to measure the structural similarity between the surface surrounding two residues. The new structural features, together with other sequence features, are used to predict RNA-binding residues using ensemble learning technique.The experimental results reveal the effectiveness of the proposed structural features. In addition, the clustering results on template patches exhibit distinct structural patterns of RNA-binding sites, although the sequences of template patches in the same cluster are not conserved. We speculate that RNAs may have structure preferences when binding with proteins.

SUBMITTER: Ren H 

PROVIDER: S-EPMC4529986 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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RNA-binding residues prediction using structural features.

Ren Huizhu H   Shen Ying Y  

BMC bioinformatics 20150809


<h4>Background</h4>RNA-protein complexes play an essential role in many biological processes. To explore potential functions of RNA-protein complexes, it's important to identify RNA-binding residues in proteins.<h4>Results</h4>In this work, we propose a set of new structural features for RNA-binding residue prediction. A set of template patches are first extracted from RNA-binding interfaces. To construct structural features for a residue, we compare its surrounding patches with each template pa  ...[more]

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