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Structural insight into mammalian sialyltransferases

TitleStructural insight into mammalian sialyltransferases
Publication TypeJournal Article
Year of Publication2009
AuthorsRao, FV, Rich, JR, Rakic, B, Buddai, S, Schwartz, MF, Johnson, K, Bowe, C, Wakarchuk, WW, DeFrees, S, Withers, SG, Strynadka, NCJ
JournalNATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume16
Pagination1186-1188
Date PublishedNOV
ISSN1545-9993
Abstract

Mammalian cell surfaces are modified by complex arrays of glycoproteins, glycolipids and polysaccharides, many of which terminate in sialic acid and have central roles in essential processes including cell recognition, adhesion and immunogenicity. Sialylation of glycoconjugates is performed by a set of sequence-related enzymes known as sialyltransferases (STs). Here we present the crystal structure of a mammalian ST, porcine ST3Gal-I, providing a structural basis for understanding the mechanism and specificity of these enzymes and for the design of selective inhibitors.

DOI10.1038/nsmb.1685