Abstract
New advances in protein post-translational modifications (PTMs) have revealed a complex layer of regulatory mechanisms through which PTMs control cell signaling and metabolic pathways, contributing to the diverse metabolic phenotypes found in cancer. Using conformational templates and the three-dimensional (3D) environment investigation of proteins in patients with colorectal cancer, it was demonstrated that most PTMs (phosphorylation, acetylation, and ubiquitination) are localized in the supersecondary structures (helical pairs). We showed that such helical pairs are represented on the outer surface of protein molecules and characterized by a largely accessible area for the surrounding solvent. Most promising and meaningful modifications were observed on the surface of vitamin D-binding protein (VDBP), complement C4-A (CO4A), X-ray repair cross-complementing protein 6 (XRCC6), Plasma protease C1 inhibitor (IC1), and albumin (ALBU), which are related to colorectal cancer developing. Based on the presented data, we propose the impact of the observed modifications in immune response, inflammatory reaction, regulation of cell migration, and promotion of tumor growth. Here, we suggest a computational approach in which high-throughput analysis for identification and characterization of PTM signature, associated with cancer metabolic reprograming, can be improved to prognostic value and bring a new strategy to the targeted therapy.
Highlights
Modern advances in systems biology and proteomics have increased interest in studying the role of post-translational modification (PTM) of proteins in pathology development mechanisms [1].The role in the implementation of biological activity of the protein has been found to be due to the three-dimensional (3D) structure and folding features [2]
Direct regulation of enzymes with diverse mechanisms is typically accomplished through the dynamic utilization of PTMs
Supersecondary structures include the development of colorectal cancer (CRC)
Summary
Modern advances in systems biology and proteomics have increased interest in studying the role of post-translational modification (PTM) of proteins in pathology development mechanisms [1].The role in the implementation of biological activity of the protein has been found to be due to the three-dimensional (3D) structure and folding features [2]. Modern advances in systems biology and proteomics have increased interest in studying the role of post-translational modification (PTM) of proteins in pathology development mechanisms [1]. PTMs produce a significant effect on a variety of cellular processes (including, but not limited to, DNA reparation, signal transduction, energy generation, and consumption, etc.) through regulation of protein activities and determining supramolecular interactions. In this regard, attempts have been made to determine the role of PTM protein in the development of various pathologies [3]
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