FIGURE 28.6. Structure and function of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs).

FIGURE 28.6

Structure and function of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs). (a) The activity of the ppGalNAcT is shown using an acceptor peptide with Ser and Thr residues and UDP-GalNAc as the donor. Some of the ppGalNAcTs may also prefer to act on the product of this reaction and use peptides with attached N-acetylgalactosamine as the acceptor. (b) The crystal structure of murine ppGalNAcT1 (mT1). The catalytic domain is shown on the left and the R-type lectin domain on the right. The β-trefoil structure and the three-lobe repeating α, β, and γ loops are indicated. The carbohydrate chain attached to the R-type domain is partly visible in the crystal. (b, Reprinted, with permission, from Fritz T.A. et al. 2004. Proc. Natl. Acad. Sci. 101: 15307–15312, ©National Academy of Sciences, U.S.A. PDB 1xh.b.)

Symbol Key: FIGURE 28.6. Structure and function of UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (ppGalNAcTs).

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From: Chapter 28, R-type Lectins

Cover of Essentials of Glycobiology
Essentials of Glycobiology. 2nd edition.
Varki A, Cummings RD, Esko JD, et al., editors.
Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009.
Copyright © 2009, The Consortium of Glycobiology Editors, La Jolla, California.

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