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Showing 1–3 of 3 results
Advanced filters: Author: Nathaniel Elsen Clear advanced filters
  • Crystallographic analysis of human O-GlcNAc hydrolase (hOGA) fragments containing the catalytic domain, including structures in complex with known inhibitors, suggests that OGA is functional as a dimer and defines opportunities for structure-based drug design.

    • Nathaniel L Elsen
    • Sangita B Patel
    • Daniel J Klein
    Research
    Nature Chemical Biology
    Volume: 13, P: 613-615
  • The ability of a protein to interact with multiple other proteins is an intriguing problem. Here, the authors use crystallography to show how a diiron hydroxylase achieves two distinct steps in the catalytic reaction, by using an overlapping binding site to recognize two different binding partners.

    • Justin F. Acheson
    • Lucas J. Bailey
    • Brian G. Fox
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-9
  • Upon the binding of small ligands, nuclear receptors regulate the transcription of genes that are associated with a number of disease mechanisms. Here, the authors report on a novel allosteric ligand binding site on the nuclear receptor RORγt.

    • Marcel Scheepstra
    • Seppe Leysen
    • Luc Brunsveld
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-10