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Predicting residue contacts for protein-protein interactions by integration of multiple information
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
- 1 Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
- 2 Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
- 3 Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
- 4 Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
- 5 Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
- 6 Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
- 7 Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Japan
- 8 Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
- 9 Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
- 10 Institute of Science and Engineering, Kanazawa University, Kanazawa, Japan
Journal of Biomedical Science and Engineering·Volume 07 (2014)·Pages 28–37·Published 2 January 2014·DOI10.4236/jbise.2014.71005
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Abstract
Detailed knowledge of interfacial region between interacting proteins is not only helpful in annotating function for proteins, but also very important for structure-based drug design and disease treatment. However, this is one of the most difficult tasks and current methods are constrained by some factors. In this study, we developed a new method to predict residue-residue contacts of two interacting protein domains by integrating information about evolutionary couplings andamino acid pairwise contact potentials, as well as domain-domain interaction interfaces. The experimental results showed that our proposed method outperformed the previous method with the same datasets. Moreover, the method promises an improvement in the source of template-based protein docking.
KeywordsResidue-Residue ContactsDomain-Domain InteractionsProtein-Protein InteractionsDomain InterfacesResidue Co-EvolutionContact Potentials
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