Projects per year
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.
Original language | English |
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Pages (from-to) | 610-612 |
Number of pages | 3 |
Journal | NATURE CHEMICAL BIOLOGY |
Volume | 13 |
Issue number | 6 |
Early online date | 27 Mar 2017 |
DOIs | |
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.Keywords
- 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
Profiles
Projects
- 1 Finished
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Structural and fragment approaches to the modulation of O-GlcNAc in cells
Davies, G. J. (Principal investigator) & Hubbard, R. E. (Co-investigator)
BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL)
29/04/13 → 31/10/16
Project: Research project (funded) › Research