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Showing 1–9 of 9 results
Advanced filters: Author: Franz Hagn Clear advanced filters

  • TGF-β is a latent complex (L-TGF-β). Latency is conferred by a homodimeric prodomain with a previously undefined domain architecture. Here we define the architecture of the prodomain as domain-swapped providing structural insights into the mechanism of activation of L-TGF-β.

    • Melina Daniilidis
    • Umut Günsel
    • Franz Hagn
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • Spider silk proteins are remarkably soluble when stored at high concentration and yet can be converted to extremely sturdy fibres, through unknown molecular mechanisms. Here, the structure of the evolutionarily conserved carboxy-terminal domain of a silk protein is presented. The results provide evidence that the structural state of this domain is essential for controlled switching between the storage and assembly forms of silk proteins. Such molecular switches might see application in the design of versatile fibrous materials.

    • Franz Hagn
    • Lukas Eisoldt
    • Horst Kessler
    Research
    Nature
    Volume: 465, P: 239-242

  • Günsel et al. unravel the structural and functional properties of OEP21, a major metabolite channel in the chloroplast outer envelope, and show that this porin utilizes a promiscuous mechanism to control the passage of a distinct set of substrates.

    • Umut Günsel
    • Kai Klöpfer
    • Franz Hagn
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 761-769

  • Hsp90 is a molecular chaperone with a wide array of client proteins, including the tumor suppressor p53. Now the structure and interaction of p53 DNA-binding domain with full-length Hsp90 or Hsp90 fragments have been studied by NMR and other biophysical methods. The results indicate that p53 interacts with multiple domains of Hsp90 and adopts a native-like state.

    • Franz Hagn
    • Stephan Lagleder
    • Horst Kessler
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1086-1093

  • Structures of GPCR neurotensin receptor 1 (NTSR1) in complex with neurotensin and Gαi1β1γ1 in a lipid bilayer environment and without stabilizing antibodies reveal extensive interactions at the GPCR–G protein interface.

    • Meng Zhang
    • Miao Gui
    • Gerhard Wagner
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 258-267

  • An experiment demonstrates that the motion of so-called skyrmions—topologically quantized magnetic whirls—causes an emergent electric field that inherits the topological quantization of the skyrmions and is directly visible in the Hall effect.

    • T. Schulz
    • R. Ritz
    • A. Rosch
    Research
    Nature Physics
    Volume: 8, P: 301-304

  • Membrane proteins can be stabilized in a native-like setting using lipid-bilayer-based nanodiscs encircled by a membrane scaffold protein. Covalently circularized nanodiscs now offer enhanced stability and control over nanodisc diameter size, improving the quality of structural data.

    • Mahmoud L Nasr
    • Diego Baptista
    • Gerhard Wagner
    Research
    Nature Methods
    Volume: 14, P: 49-52

  • The applications of solution-state NMR of membrane proteins are often limited by difficulty in finding a suitable membrane mimetic of tailored size that shows native-like membrane properties and provides long-term stability. This protocol describes how to assemble phospholipid nanodiscs and incorporate membrane proteins for NMR-structural studies.

    • Franz Hagn
    • Mahmoud L Nasr
    • Gerhard Wagner
    Protocols
    Nature Protocols
    Volume: 13, P: 79-98