Roth, C, Chan, S, Offen, WA et al. (7 more authors) (2017) Structural and functional insight into human O-GlcNAcase. Nature Chemical Biology, 13 (6). pp. 610-612. ISSN 1552-4469
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 a paper published in Nature Chemical Biology. Uploaded in accordance with the publisher’s self-archiving policy. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 08 Jun 2017 15:40 |
Last Modified: | 28 Sep 2017 12:05 |
Status: | Published |
Publisher: | Nature Publishing Group |
Identification Number: | 10.1038/nchembio.2358 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:117506 |