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dc.contributor.authorGrewal, Ravneet Kaur
dc.contributor.authorShaikh, Abdul Rajjak
dc.contributor.authorGorle, Suresh
dc.contributor.authorKaur, Manjeet
dc.contributor.authorVideira, Paula Alexendra
dc.contributor.authorCavallo, Luigi
dc.contributor.authorChawla, Mohit
dc.date.accessioned2021-09-07T12:49:51Z
dc.date.available2021-09-07T12:49:51Z
dc.date.issued2021-08-27
dc.date.submitted2021-06-17
dc.identifier.citationGrewal, R. K., Shaikh, A. R., Gorle, S., Kaur, M., Videira, P. A., Cavallo, L., & Chawla, M. (2021). Structural Insights in Mammalian Sialyltransferases and Fucosyltransferases: We Have Come a Long Way, but It Is Still a Long Way Down. Molecules, 26(17), 5203. doi:10.3390/molecules26175203
dc.identifier.issn1420-3049
dc.identifier.doi10.3390/molecules26175203
dc.identifier.urihttp://hdl.handle.net/10754/671093
dc.description.abstractMammalian 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.
dc.description.sponsorshipThe APC was funded by King Abdullah University of Science and Technology. M.C.: L.C. and A.R.S. acknowledge the King Abdullah University of Science and Technology (KAUST) for support. We thank Romina Oliva, University of Parthenope (Naples), for helpful comments. Thanks to the STEMskills Research and Education Lab team members for support.
dc.publisherMDPI AG
dc.relation.urlhttps://www.mdpi.com/1420-3049/26/17/5203
dc.rightsThis article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleStructural insights in mammalian sialyltransferases and fucosyltransferases: We have come a long way, but it is still a long way down
dc.typeArticle
dc.contributor.departmentKAUST Catalysis Center (KCC)
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.contributor.departmentChemical Science Program
dc.identifier.journalMolecules
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionSTEMskills Research and Education Lab Private Limited, Faridabad, 121002, Haryana, India
dc.contributor.institutionDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA
dc.contributor.institutionBiotechnology Engineering, University Institute of Engineering & Technology (UIET), Maharshi Dayanand University, Rohtak, 124001, Haryana, India
dc.contributor.institutionAssociate Laboratory i4HB—Institute for Health and Bioeconomy, NOVA School of Science and Technology, NOVA University Lisbon, 2819-516, Caparica, Portugal
dc.contributor.institutionUCIBIO—Applied Molecular Biosciences Unit, Department of Life Sciences, NOVA School of Science and Technology, NOVA University Lisbon, 2819-516, Caparica, Portugal
dc.contributor.institutionCDG & Allies—Professionals and Patient Associations International Network (CDG & Allies—PPAIN), 2829-516, Caparica, Portugal
dc.identifier.volume26
dc.identifier.issue17
dc.identifier.pages5203
kaust.personShaikh, Abdul Rajjak
kaust.personCavallo, Luigi
kaust.personChawla, Mohit
dc.date.accepted2021-08-20
dc.identifier.eid2-s2.0-85113933396
refterms.dateFOA2021-09-07T12:52:12Z


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This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.
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