Inferring domain-domain interactions from protein-protein interactions
Proceedings of the sixth annual international conference on Computational biology
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The current need for high-throughput protein interaction detection has resulted in interaction data being generated en masse, using experimental methods such as yeast-two-hybrids and protein chips. Such data can be errorful and they often do not provide adequate functional information for the detected interactions; it is therefore useful to develop an in silico approach to further validate and annotate the detected protein interactions. Given that protein-protein interactions involve physical interactions between protein domains, domain-domain interaction information can be useful for validating, annotating, and even predicting protein interactions. However, large-scale experimentally determined domain-domain interaction data do not exist; as such, we describe an integrative approach to computationally derive putative domain interactions from multiple data sources, including rosetta stone sequences, protein interactions, and protein complexes. We show the usefulness of such an integrative approach by applying the derived domain interactions to predict and validate protein-protein interactions.