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Literature DB >> 28346407

Insights into activity and inhibition from the crystal structure of human O-GlcNAcase.

Nathaniel L Elsen¹, Sangita B Patel², Rachael E Ford¹, Dawn L Hall¹, Fred Hess³, Hari Kandula¹, Maria Kornienko¹, John Reid², Harold Selnick⁴, Jennifer M Shipman¹, Sujata Sharma¹, Kevin J Lumb¹, Stephen M Soisson², Daniel J Klein².

Abstract

O-GlcNAc hydrolase (OGA) catalyzes removal of βα-linked N-acetyl-D-glucosamine from serine and threonine residues. We report crystal structures of Homo sapiens OGA catalytic domain in apo and inhibited states, revealing a flexible dimer that displays three unique conformations and is characterized by subdomain α-helix swapping. These results identify new structural features of the substrate-binding groove adjacent to the catalytic site and open new opportunities for structural, mechanistic and drug discovery activities.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 2017 PMID： 28346407 DOI： 10.1038/nchembio.2357

Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040

32 in total

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8. Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain.

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Review 6. Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.

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