Structural and functional insight into human O-GlcNAcase View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-03-27

AUTHORS

Christian Roth, Sherry Chan, Wendy A Offen, Glyn R Hemsworth, Lianne I Willems, Dustin T King, Vimal Varghese, Robert Britton, David J Vocadlo, Gideon J Davies

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. More... »

PAGES

610-612

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchembio.2358

DOI

http://dx.doi.org/10.1038/nchembio.2358

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1084128752

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28346405


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