Document Type
Article
Publication Date
2017
College/Unit
Eberly College of Arts and Sciences
Department/Program/Center
Microbiology, Immunology, and Cell Biology
Abstract
Traditional Protein-Protein Interaction (PPI) networks, which use a node and edge representation, lack some valuable information about the mechanistic details of biological processes. Mapping protein structures to these PPI networks not only provides structural details of each interaction but also helps us to find the mutual exclusive interactions. Yet it is not a comprehensive representation as it neglects the conformational changes of proteins which may lead to different interactions, functions, and downstream signalling. In this study, we proposed a new representation for structural PPI networks inspecting the alternative conformations of proteins. We performed a large-scale study by creating breast cancer metastasis network and equipped it with different conformers of proteins. Our results showed that although 88% of proteins in our network has at least two structures in Protein Data Bank (PDB), only 22% of them have alternative conformations and the remaining proteins have different regions saved in PDB. However, using even this small set of alternative conformations we observed a considerable increase in our protein docking predictions. Our protein-protein interaction predictions increased from 54% to 76% using the alternative conformations. We also showed the benefits of investigating structural data and alternative conformations of proteins through three case studies.
Digital Commons Citation
Halakou, Farideh; Kilic, Emel S.; Cukuroglu, Engin; Keskin, Ozlem; and Gursoy, Attila, "Enriching Traditional Protein-protein Interaction Networks with Alternative Conformations of Proteins" (2017). Faculty & Staff Scholarship. 1549.
https://researchrepository.wvu.edu/faculty_publications/1549
Source Citation
Halakou, F., Kilic, E.S., Cukuroglu, E. et al. Enriching Traditional Protein-protein Interaction Networks with Alternative Conformations of Proteins. Sci Rep 7, 7180 (2017). https://doi.org/10.1038/s41598-017-07351-0
Comments
Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.