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- W2603194836 abstract "Crystal structures of human O-GlcNAc hydrolase (hOGA) fragments show that hOGA's dimeric structure is organized by swapping of an α-helical element and reveal features of inhibitor binding to the catalytic domain. 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." @default.
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- W2603194836 date "2017-03-27" @default.
- W2603194836 modified "2023-10-17" @default.
- W2603194836 title "Structural and functional insight into human O-GlcNAcase" @default.
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- W2603194836 doi "https://doi.org/10.1038/nchembio.2358" @default.
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