Structural and functional insight into human O-GlcNAcase

Christian Roth*, Oi Yi Chan, Wendy Anne Offen, Glyn Robert Hemsworth, Lianne Irene Willems, Dustin T. King, Vimal Varghese, Robert Britton, David J. Vocadlo, Gideon John Davies

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value.
Original languageEnglish
Pages (from-to)610-612
Number of pages3
Issue number6
Early online date27 Mar 2017
Publication statusPublished - 1 Jun 2017

Bibliographical note

© 2017, Nature America, Inc. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.


  • Acetylglucosamine/metabolism
  • Binding Sites
  • Enzyme Activation/drug effects
  • Enzyme Inhibitors/pharmacology
  • HEK293 Cells
  • Humans
  • Ligands
  • Models, Molecular
  • Protein Binding
  • Protein Isoforms/chemistry
  • Protein Structure, Tertiary
  • beta-N-Acetylhexosaminidases/chemistry

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