Search Results

You searched for all publications:

with publication states 'Published (Approved)'

Search Again...

These results only include publications that have been reviewed and processed by Diamond Light Source. To also view papers that have not yet been processed click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

12 items found (0 items not approved), displaying 11 to 12.[First/Prev] 1, 2 [Next/Last]

Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Bisubstrate UDPpeptide conjugates as human O-GlcNAc transferase inhibitors Vladimir s. Borodkin , Marianne Schimpl , Mehmet Gundogdu , Karim Rafie , Helge Dorfmueller , David Robinson , Daniel Van Aalten Biochemical Journal 457, 497 - 502 DOI: 10.1042/BJ20131272 Diamond Proposal Number(s): [8268] Open Access Show Abstract ▼ Abstract: Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation. We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring. Goblin1 co-crystallizes with OGT, revealing an ordered C3 linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.	Feb 2014
I03-Macromolecular Crystallography	Synergy of Peptide and Sugar in O-GlcNAcase Substrate Recognition Marianne Schimpl , Vladimir s. Borodkin , Lindsey j. Gray , Daan m.f. Van aalten Chemistry & Biology 19 (2), 173 - 178 DOI: 10.1016/j.chembiol.2012.01.011 PMID: 22365600 Diamond Proposal Number(s): [1223] Open Access Show Abstract ▼ Abstract: Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes. O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively. We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome. Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation. In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains. These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome. In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site.	Feb 2012

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User