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Structural and functional insight into human O-GlcNAcase

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JournalNATURE CHEMICAL BIOLOGY
DateAccepted/In press - 9 Mar 2017
DateE-pub ahead of print - 27 Mar 2017
DatePublished (current) - 1 Jun 2017
Volume13
Number of pages3
Pages (from-to)610-612
Early online date27/03/17
Original languageEnglish

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.

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© 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.

    Research areas

  • 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

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