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Structural insight into mammalian sialyltransferases

Nature Structural & Molecular Biology volume 16, pages 1186–1188 (2009)Cite this article

Abstract

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.

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Figure 1: The GT29 fold.
Figure 2: The GT29 active site.

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada

    Francesco V Rao, Stephen G Withers & Natalie C J Strynadka

  2. Centre for Blood Research, University of British Columbia, Vancouver, Canada

    Francesco V Rao & Natalie C J Strynadka

  3. Department of Chemistry, University of British Columbia, Vancouver, Canada

    Francesco V Rao, Jamie R Rich, Bojana Rakić & Stephen G Withers

  4. Neose Technologies, Inc., Horsham, Pennsylvania, USA

    Sai Buddai, Marc F Schwartz, Karl Johnson, Caryn Bowe & Shawn DeFrees

  5. Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada

    Warren W Wakarchuk

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  1. Francesco V Rao
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Correspondence to Natalie C J Strynadka.

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Supplementary Figures 1–4, Supplementary Tables 1 and 2 and Supplementary Methods (PDF 805 kb)

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Rao, F., Rich, J., Rakić, B. et al. Structural insight into mammalian sialyltransferases. Nat Struct Mol Biol 16, 1186–1188 (2009). https://doi.org/10.1038/nsmb.1685

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