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DDI2PPI: an integrated web server for protein-protein interaction and residue contact matrix predictions

Published: 20 September 2014 Publication History

Abstract

Protein-protein interactions (PPIs) play essential roles in many biological processes. The large gap between the fast growing protein sequence information and the experimentally verified PPI information has motivated the development of computational methods to predict PPIs and residue-residue (RR) contacts. Although many tools are available for PPI predictions, most do not make a distinction between direct PPIs, which refer to physical contacts between two proteins, and indirect PPIs. Furthermore, few tools predict detailed RR contacts between interacting proteins, which are valuable for understanding chemical interaction mechanisms and designing investigations of the interaction. Here we present the web server DDI2PPI to provide PPI and RR contact matrix predictions from query protein sequences, focusing on predicting direct physical interactions. DDI2PPI implements algorithms that predict PPIs and RR contact matrices through domain-domain interaction (DDI) analysis based on interaction profile Hidden Markov Models (ipHMMs) and Support Vector Machines (SVMs). It covers more than 6000 DDI families in 3DID, a database of three-dimensional interacting domains. DDI2PPI (version 1.0) is freely available at http://annotation.dbi.udel.edu/ppi_prediction/.

References

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Aloy, P. and Russell, R. B., 2003. InterPreTS: protein interaction prediction through tertiary structure. Bioinformatics 19, 1, 161--162.
[2]
González, A. J. and Liao, L., 2009. Constrained Fisher scores derived from interaction profile hidden Markov models improve protein to protein interaction prediction. In Bioinformatics and Computational Biology Springer, 236--247.
[3]
González, A. J. and Liao, L., 2010. Predicting domain-domain interaction based on domain profiles with feature selection and support vector machines. BMC bioinformatics 11, 1, 537.
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González, A. J., Liao, L., and Wu, C. H., 2013. Prediction of contact matrix for protein--protein interaction. Bioinformatics 29, 8, 1018--1025.
[5]
Mosca, R., Céol, A., Stein, A., Olivella, R., and Aloy, P., 2014. 3did: a catalog of domain-based interactions of known three-dimensional structure. Nucleic acids research 42, D1 (January 1, 2014), D374--D379. DOI= http://dx.doi.org/10.1093/nar/gkt887.
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Wojcik, J. and Schächter, V., 2001. Protein-protein interaction map inference using interacting domain profile pairs. Bioinformatics 17, suppl 1, S296--S305.
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Zhou, H.-X. and Shan, Y., 2001. Prediction of protein interaction sites from sequence profile and residue neighbor list. Proteins: Structure, Function, and Bioinformatics 44, 3, 336--343. DOI= http://dx.doi.org/10.1002/prot.1099.

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  1. DDI2PPI: an integrated web server for protein-protein interaction and residue contact matrix predictions

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        cover image ACM Conferences
        BCB '14: Proceedings of the 5th ACM Conference on Bioinformatics, Computational Biology, and Health Informatics
        September 2014
        851 pages
        ISBN:9781450328944
        DOI:10.1145/2649387
        • General Chairs:
        • Pierre Baldi,
        • Wei Wang
        Permission to make digital or hard copies of part or all of this work for personal or classroom use is granted without fee provided that copies are not made or distributed for profit or commercial advantage and that copies bear this notice and the full citation on the first page. Copyrights for third-party components of this work must be honored. For all other uses, contact the Owner/Author.

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        New York, NY, United States

        Publication History

        Published: 20 September 2014

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        Author Tags

        1. contact matrix
        2. domain-domain interaction
        3. machine learning
        4. prediction
        5. protein-protein interaction
        6. residue-residue contact
        7. server

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        BCB '14
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        BCB '14: ACM-BCB '14
        September 20 - 23, 2014
        California, Newport Beach

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        Overall Acceptance Rate 254 of 885 submissions, 29%

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