Detecting mutually exclusive interactions in protein-protein interaction maps.
Type
ArticleKAUST Grant Number
KUK-I1-012-43Date
2012-06-08Permanent link to this record
http://hdl.handle.net/10754/596839
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Comprehensive protein interaction maps can complement genetic and biochemical experiments and allow the formulation of new hypotheses to be tested in the system of interest. The computational analysis of the maps may help to focus on interesting cases and thereby to appropriately prioritize the validation experiments. We show here that, by automatically comparing and analyzing structurally similar regions of proteins of known structure interacting with a common partner, it is possible to identify mutually exclusive interactions present in the maps with a sensitivity of 70% and a specificity higher than 85% and that, in about three fourth of the correctly identified complexes, we also correctly recognize at least one residue (five on average) belonging to the interaction interface. Given the present and continuously increasing number of proteins of known structure, the requirement of the knowledge of the structure of the interacting proteins does not substantially impact on the coverage of our strategy that can be estimated to be around 25%. We also introduce here the Estrella server that embodies this strategy, is designed for users interested in validating specific hypotheses about the functional role of a protein-protein interaction and it also allows access to pre-computed data for seven organisms.Citation
Sánchez Claros C, Tramontano A (2012) Detecting Mutually Exclusive Interactions in Protein-Protein Interaction Maps. PLoS ONE 7: e38765. Available: http://dx.doi.org/10.1371/journal.pone.0038765.Sponsors
Award number KUK-I1-012-43 made by King Abdullah University of Science and Technology (KAUST). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Publisher
Public Library of Science (PLoS)Journal
PLoS ONEPubMed ID
22715412PubMed Central ID
PMC3370996ae974a485f413a2113503eed53cd6c53
10.1371/journal.pone.0038765
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