Computational Analysis of the Stability of SCF Ligases Employing Domain Information
Proceedings of the 5th ACM Conference on Bioinformatics, Computational Biology, and Health Informatics
Because of the unequivocally fundamental role of SCF ubiquitin ligase in many biological functions within a living cell including regulating DNA repair, cell cycle progression, and inflammation, we have analyzed the role of domain interactions in determining particular types of protein-protein interactions (PPIs) that are known or predicted to occur involving subunit components of the SCF-ligase complex. We focus on the prediction and analysis of obligate and non-obligate SCF-ligase complexes by using sequence domains from the Pfam database. After extracting different types of feature vectors, the prediction is performed via a support vector machine (SVM). The numerical results demonstrate that most of the interactions of SCF-ligase complexes are mediated by at least one domain. Moreover, domain-domain interactions dominate in obligate complexes whereas non-obligate complexes exhibit more domain-peptide chain interactions. Also, the computational results show that the best prediction accuracy of 80.46% is achieved using the combination of feature vectors of domain-domain type, domain-peptide chain type and no-domain interactions.
Maleki, Mina; Rueda, Luis; Dezfulian, Mohammad Haj; and Crosby, William L., "Computational Analysis of the Stability of SCF Ligases Employing Domain Information" (2014). Proceedings of the 5th ACM Conference on Bioinformatics, Computational Biology, and Health Informatics, 625-626.