Structural insight into mammalian sialyltransferases

Nat Struct Mol Biol. 2009 Nov;16(11):1186-8. doi: 10.1038/nsmb.1685. Epub 2009 Oct 11.

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 sequence-related 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.

MeSH terms

  • Animals
  • Catalytic Domain
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • N-Acetylneuraminic Acid / metabolism
  • Protein Structure, Secondary
  • Sialyltransferases / chemistry*
  • Sialyltransferases / genetics
  • Sialyltransferases / metabolism
  • Substrate Specificity
  • Swine

Substances

  • Sialyltransferases
  • beta-galactoside alpha-2,3-sialyltransferase
  • N-Acetylneuraminic Acid

Associated data

  • PDB/2WML
  • PDB/2WNB
  • PDB/2WNF