Brief Communication abstract
Nature Structural & Molecular Biology 16, 1186 - 1188 (2009)
Published online: 11 October 2009 | doi:10.1038/nsmb.1685
Structural insight into mammalian sialyltransferases
Francesco V Rao1,2,3,
Jamie R Rich3,
Bojana Raki
3,
Sai Buddai4,
Marc F Schwartz4,
Karl Johnson4,
Caryn Bowe4,
Warren W Wakarchuk5,
Shawn DeFrees4,
Stephen G Withers1,3
&
Natalie C J Strynadka1,2
Sialic acid is the most abundant terminal monosaccharide on mammalian cell surface glycoconjugates. The crystal structures of a mammalian sialyltransferase, that of porcine ST3Gal-I, in the apo form and bound to analogues of the donor and acceptor substrate are now described, providing insights into the catalytic mechanism and for inhibitor design.
- Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.
- Centre for Blood Research, University of British Columbia, Vancouver, Canada.
- Department of Chemistry, University of British Columbia, Vancouver, Canada.
- Neose Technologies, Inc., Horsham, Pennsylvania, USA.
- Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada.
Correspondence to: Natalie C J Strynadka1,2 e-mail: natalie@byron.biochem.ubc.ca
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