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Review

Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down

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STEMskills Research and Education Lab Private Limited, Faridabad 121002, Haryana, India
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Kaust Catalysis Center, Physical Sciences and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia
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Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA
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Biotechnology Engineering, University Institute of Engineering & Technology (UIET), Maharshi Dayanand University, Rohtak 124001, Haryana, India
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Associate Laboratory i4HB—Institute for Health and Bioeconomy, NOVA School of Science and Technology, NOVA University Lisbon, 2819-516 Caparica, Portugal
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UCIBIO—Applied Molecular Biosciences Unit, Department of Life Sciences, NOVA School of Science and Technology, NOVA University Lisbon, 2819-516 Caparica, Portugal
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CDG & Allies—Professionals and Patient Associations International Network (CDG & Allies—PPAIN), 2829-516 Caparica, Portugal
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Authors to whom correspondence should be addressed.
Academic Editor: Stefan Janecek
Molecules 2021, 26(17), 5203; https://doi.org/10.3390/molecules26175203
Received: 17 June 2021 / Revised: 19 August 2021 / Accepted: 20 August 2021 / Published: 27 August 2021
(This article belongs to the Special Issue Recent Advances in Carbohydrate-Active Enzymes)
Mammalian cell surfaces are modified with complex arrays of glycans that play major roles in health and disease. Abnormal glycosylation is a hallmark of cancer; terminal sialic acid and fucose in particular have high levels in tumor cells, with positive implications for malignancy. Increased sialylation and fucosylation are due to the upregulation of a set of sialyltransferases (STs) and fucosyltransferases (FUTs), which are potential drug targets in cancer. In the past, several advances in glycostructural biology have been made with the determination of crystal structures of several important STs and FUTs in mammals. Additionally, how the independent evolution of STs and FUTs occurred with a limited set of global folds and the diverse modular ability of catalytic domains toward substrates has been elucidated. This review highlights advances in the understanding of the structural architecture, substrate binding interactions, and catalysis of STs and FUTs in mammals. While this general understanding is emerging, use of this information to design inhibitors of STs and FUTs will be helpful in providing further insights into their role in the manifestation of cancer and developing targeted therapeutics in cancer. View Full-Text
Keywords: sialyltransferase; fucosyltransferase; glyocosyltransferases in cancer; drug design sialyltransferase; fucosyltransferase; glyocosyltransferases in cancer; drug design
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MDPI and ACS Style

Grewal, R.K.; Shaikh, A.R.; Gorle, S.; Kaur, M.; Videira, P.A.; Cavallo, L.; Chawla, M. Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down. Molecules 2021, 26, 5203. https://doi.org/10.3390/molecules26175203

AMA Style

Grewal RK, Shaikh AR, Gorle S, Kaur M, Videira PA, Cavallo L, Chawla M. Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down. Molecules. 2021; 26(17):5203. https://doi.org/10.3390/molecules26175203

Chicago/Turabian Style

Grewal, Ravneet K., Abdul R. Shaikh, Suresh Gorle, Manjeet Kaur, Paula A. Videira, Luigi Cavallo, and Mohit Chawla. 2021. "Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down" Molecules 26, no. 17: 5203. https://doi.org/10.3390/molecules26175203

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