Structural insight into mammalian sialyltransferases

DOI	Resolve DOI: https://doi.org/10.1038/nsmb.1685
Author	Search for: Rao, Francesco V.; Search for: Rich, Jamie R.; Search for: Rakic, Bojana; Search for: Buddai, Sai; Search for: Schwartz, Marc F.; Search for: Johnson, Karl; Search for: Bowe, Caryn; Search for: Wakarchuk, Warren W.¹; Search for: Defrees, Shawn; Search for: Withers, Stephen G.; Search for: Strynadka, Natalie C.J.
Affiliation	National Research Council of Canada. NRC Institute for Biological Sciences
Format	Text, Article
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 sequencerelated 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.
Publication date	2009-10-11
In	Nature Structural and Molecular Biology 16, no. 11 (11 October 2009): 1186–1188.
Language	English
Peer reviewed	Yes
NPARC number	15295292
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Record identifier	c1a61f5f-432b-4b5f-8a01-662ae53abf40
Record created	2010-05-17
Record modified	2020-04-16