Next Article in Journal
Ezrin Phosphorylation at T567 Modulates Cell Migration, Mechanical Properties, and Cytoskeletal Organization
Previous Article in Journal
Epigallocatechin-3-Gallate Suppresses Vasculogenic Mimicry through Inhibiting the Twist/VE-Cadherin/AKT Pathway in Human Prostate Cancer PC-3 Cells
Previous Article in Special Issue
Translational Regulation of Pmt1 and Pmt2 by Bfr1 Affects Unfolded Protein O-Mannosylation
Open AccessReview

3D Structure and Function of Glycosyltransferases Involved in N-glycan Maturation

1
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan
2
Faculty of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, Miyagi 981-8558, Japan
3
Department of Glyco-Oncology and Medical Biochemistry, Osaka International Cancer Institute, 3-1-69 Otemae, Chuo-ku, Osaka 541-8567, Japan
4
Center for Highly Advanced Integration of Nano and Life Sciences (G-CHAIN), Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(2), 437; https://doi.org/10.3390/ijms21020437
Received: 17 December 2019 / Revised: 6 January 2020 / Accepted: 8 January 2020 / Published: 9 January 2020
Glycosylation is the most ubiquitous post-translational modification in eukaryotes. N-glycan is attached to nascent glycoproteins and is processed and matured by various glycosidases and glycosyltransferases during protein transport. Genetic and biochemical studies have demonstrated that alternations of the N-glycan structure play crucial roles in various physiological and pathological events including progression of cancer, diabetes, and Alzheimer’s disease. In particular, the formation of N-glycan branches regulates the functions of target glycoprotein, which are catalyzed by specific N-acetylglucosaminyltransferases (GnTs) such as GnT-III, GnT-IVs, GnT-V, and GnT-IX, and a fucosyltransferase, FUT8s. Although the 3D structures of all enzymes have not been solved to date, recent progress in structural analysis of these glycosyltransferases has provided insights into substrate recognition and catalytic reaction mechanisms. In this review, we discuss the biological significance and structure-function relationships of these enzymes. View Full-Text
Keywords: N-glycosylation; glycosyltransferase; atomic structure; GT-A fold; GT-B fold N-glycosylation; glycosyltransferase; atomic structure; GT-A fold; GT-B fold
Show Figures

Figure 1

MDPI and ACS Style

Nagae, M.; Yamaguchi, Y.; Taniguchi, N.; Kizuka, Y. 3D Structure and Function of Glycosyltransferases Involved in N-glycan Maturation. Int. J. Mol. Sci. 2020, 21, 437.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop