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Insights into activity and inhibition from the crystal structure of human O-GlcNAcase.
- Source :
-
Nature chemical biology [Nat Chem Biol] 2017 Jun; Vol. 13 (6), pp. 613-615. Date of Electronic Publication: 2017 Mar 27. - Publication Year :
- 2017
-
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.
- Subjects :
- Acetylglucosamine metabolism
Binding Sites
Calorimetry
Catalytic Domain
Crystallography, X-Ray
Enzyme Activation drug effects
Enzyme Inhibitors pharmacology
Humans
Protein Structure, Tertiary
Substrate Specificity
Models, Biological
beta-N-Acetylhexosaminidases chemistry
beta-N-Acetylhexosaminidases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1552-4469
- Volume :
- 13
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Nature chemical biology
- Publication Type :
- Academic Journal
- Accession number :
- 28346407
- Full Text :
- https://doi.org/10.1038/nchembio.2357