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Structural and functional insight into human O-GlcNAcase
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Publication details
| Journal | NATURE CHEMICAL BIOLOGY |
|---|---|
| Date | Accepted/In press - 9 Mar 2017 |
| Date | E-pub ahead of print - 27 Mar 2017 |
| Date | Published (current) - 1 Jun 2017 |
| Issue number | 6 |
| Volume | 13 |
| Number of pages | 3 |
| Pages (from-to) | 610-612 |
| Early online date | 27/03/17 |
| Original language | English |
Abstract
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.
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
Research areas
Projects
Structural and fragment approaches to the modulation of O-GlcNAc in cells
Project: Research project (funded) › Research
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