Roth, Christian orcid.org/0000-0001-5806-0987, Chan, Oi Yi, Offen, Wendy Anne orcid.org/0000-0002-2758-4531 et al. (7 more authors) (2017) Structural and functional insight into human O-GlcNAcase. NATURE CHEMICAL BIOLOGY. pp. 610-612. ISSN 1552-4450
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 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 |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Funding Information: | Funder Grant number BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL) BB/K003836/1 |
Depositing User: | Pure (York) |
Date Deposited: | 03 May 2017 11:20 |
Last Modified: | 17 Dec 2024 00:07 |
Published Version: | https://doi.org/10.1038/nchembio.2358 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1038/nchembio.2358 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:115951 |
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