2xpk

Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidasesCell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases

Structural highlights 2xpk is a 2 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OGA_CLOP1 Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Publication Abstract from PubMed Posttranslational modification of metazoan nucleocytoplasmic proteins with N-acetylglucosamine (O-GlcNAc) is essential, dynamic, and inducible and can compete with protein phosphorylation in signal transduction. Inhibitors of O-GlcNAcase, the enzyme removing O-GlcNAc, are useful tools for studying the role of O-GlcNAc in a range of cellular processes. We report the discovery of nanomolar OGA inhibitors that are up to 900,000-fold selective over the related lysosomal hexosaminidases. When applied at nanomolar concentrations on live cells, these cell-penetrant molecules shift the O-GlcNAc equilibrium toward hyper-O-GlcNAcylation with EC values down to 3 nM and are thus invaluable tools for the study of O-GlcNAc cell biology. Cell-penetrant, nanomolar O-GlcNAcase inhibitors selective against lysosomal hexosaminidases.,Dorfmueller HC, Borodkin VS, Schimpl M, Zheng X, Kime R, Read KD, van Aalten DM Chem Biol. 2010 Nov 24;17(11):1250-5. PMID:21095575 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-Hexosaminidase Beta-Hexosaminidase 3D structures O-GlcNAcase

spinqualitylabelsall models 2xpk, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image