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Open AccessEditor’s ChoiceArticle

Super Secondary Structures of Proteins with Post-Translational Modifications in Colon Cancer

1
Institute of Mathematical Problems of Biology RAS-the Branch of Keldysh Institute of Applied Mathematics of Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
2
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
3
V.N. Orekhovich Institute of Biomedical Chemistry, 119121 Moscow, Russia
*
Author to whom correspondence should be addressed.
Academic Editors: Susy Piovesana and Rudy J. Richardson
Molecules 2020, 25(14), 3144; https://doi.org/10.3390/molecules25143144
Received: 1 June 2020 / Revised: 22 June 2020 / Accepted: 6 July 2020 / Published: 9 July 2020
(This article belongs to the Section Molecular Structure)
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. View Full-Text
Keywords: colorectal cancer; ultrahigh-resolution mass spectrometry; post-translational modifications; helical pair; protein structural motifs; supersecondary structure colorectal cancer; ultrahigh-resolution mass spectrometry; post-translational modifications; helical pair; protein structural motifs; supersecondary structure
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MDPI and ACS Style

Tikhonov, D.; Kulikova, L.; Kopylov, A.; Malsagova, K.; Stepanov, A.; Rudnev, V.; Kaysheva, A. Super Secondary Structures of Proteins with Post-Translational Modifications in Colon Cancer. Molecules 2020, 25, 3144. https://doi.org/10.3390/molecules25143144

AMA Style

Tikhonov D, Kulikova L, Kopylov A, Malsagova K, Stepanov A, Rudnev V, Kaysheva A. Super Secondary Structures of Proteins with Post-Translational Modifications in Colon Cancer. Molecules. 2020; 25(14):3144. https://doi.org/10.3390/molecules25143144

Chicago/Turabian Style

Tikhonov, Dmitry; Kulikova, Liudmila; Kopylov, Arthur; Malsagova, Kristina; Stepanov, Alexander; Rudnev, Vladimir; Kaysheva, Anna. 2020. "Super Secondary Structures of Proteins with Post-Translational Modifications in Colon Cancer" Molecules 25, no. 14: 3144. https://doi.org/10.3390/molecules25143144

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