Structural insight into mammalian sialyltransferases

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DOIResolve DOI: http://doi.org/10.1038/nsmb.1685
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TypeArticle
Journal titleNature Structural and Molecular Biology
Volume16
Issue11
Pages11861188; # of pages: 3
AbstractMammalian 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
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences
Peer reviewedYes
NPARC number15295292
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Record identifierc1a61f5f-432b-4b5f-8a01-662ae53abf40
Record created2010-05-17
Record modified2016-05-09
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