Projects per year
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.
|Number of pages||3|
|Journal||NATURE CHEMICAL BIOLOGY|
|Early online date||27 Mar 2017|
|Publication status||Published - 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.
- Binding Sites
- Enzyme Activation/drug effects
- Enzyme Inhibitors/pharmacology
- HEK293 Cells
- Models, Molecular
- Protein Binding
- Protein Isoforms/chemistry
- Protein Structure, Tertiary
Gideon John Davies, FRS, FMedSci
- Chemistry - Professor
Lianne Irene Willems
- Chemistry - Lecturer in Glycoscience
- 1 Finished
Structural and fragment approaches to the modulation of O-GlcNAc in cells
Davies, G. J. & Hubbard, R. E.
29/04/13 → 31/10/16
Project: Research project (funded) › Research