Introduction: O-glcnacylation, as an important post-translational modification , plays a protective role in Alzheimer's disease by inhibiting brain apoptotic necrosis caused by the aggregation of tau. To elucidate the specificity of substrate recognition and binding in O-GlCNAcylation, as well as the inhibition mechanism of small molecule inhibitors, we have resolved the structure of OGA and its complex and thus developed an electrophilic probe that can rapidly identify key amino acids of substrate binding based on the OGT’s 3D structure we got. It is of great significance for the understanding of O-GlcnAcylation modification and its status as a novel target of Alzheimer's disease, and provide an important basis for the development and design of novel Alzheimer's disease therapeutics.
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