Brief Communication abstract


Nature Chemical Biology 4, 200 - 202 (2008)
Published online: 27 January 2008 | doi:10.1038/nchembio.66

Engineering sulfotransferases to modify heparan sulfate

Ding Xu1, Andrea F Moon2, Danyin Song1, Lars C Pedersen2 & Jian Liu1

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The biosynthesis of heparan sulfate (HS) involves an array of specialized sulfotransferases. Here, we present a study aimed at engineering the substrate specificity of different HS 3-O-sulfotransferase isoforms. Based on the crystal structures, we identified a pair of amino acid residues responsible for selecting the substrates. Mutations of these residues altered the substrate specificities. Our results demonstrate the feasibility of tailoring the specificity of sulfotransferases to modify HS with desired functions.

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  1. Division of Medicinal Chemistry and Natural Products, School of Pharmacy, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
  2. Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, 111 T.W. Alexander Drive, Research Triangle Park, North Carolina 27709, USA.

Correspondence to: Jian Liu1 e-mail: jian_liu@unc.edu



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