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Showing 1–9 of 9 results
Advanced filters: Author: Ute A. Hellmich Clear advanced filters

  • It is well established that proteins in the TRP family of ion channels assemble from four subunits. But do they always do this? A five-subunit structure has now been observed, and might be involved in channel regulation.

    • Ute A. Hellmich
    News & Views
    Nature
    Volume: 621, P: 46-47

  • An integrated structural biology approach uncovers the structural complexity of the intrinsically disordered region (IDR) within the TRPV4 ion channel. Multiple stimulatory and inhibitory elements were identified within the IDR that modulate channel activity in a lipid-dependent manner.

    • Benedikt Goretzki
    • Christoph Wiedemann
    • Ute A. Hellmich
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-20

  • Magic-angle spinning ssNMR used to monitor the E. coli integral membrane protein DGK reconstituted into lipid bilayers reveals the kinetics and mechanisms of this enzyme in both the membrane phase where diacylglycerol is converted to PA and in the aqueous phase where ATP is converted to ADP.

    • Sandra J Ullrich
    • Ute A Hellmich
    • Clemens Glaubitz
    Research
    Nature Chemical Biology
    Volume: 7, P: 263-270

  • Spider silk is of interest in material science research. Here the authors show that the tight binding of a spider silk protein domain relies on the amino acid methionine, which is abundant in the domain core where it facilitates dynamic shape adaption of the binding interface.

    • Julia C. Heiby
    • Benedikt Goretzki
    • Hannes Neuweiler
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • TRPV2 is activated by temperature and cannabinoids. Here, the authors have used cryo-EM and electrophysiology to identify a cannabinoid binding site distinct from that of cannabidiol as a possible drug target for treatment of inflammation and immune-mediated diseases.

    • Liying Zhang
    • Charlotte Simonsen
    • Peter M. Zygmunt
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-18

  • TRPV4 dominant mutations cause neuropathy. Here, the authors show that TRPV4 binds and interacts with RhoA, modulating the actin cytoskeleton. Neuropathy-causing mutations of TRPV4 disrupt this complex, leading to RhoA activation and impairment of neurite extension in cultured cells and flies.

    • Brett A. McCray
    • Erika Diehl
    • Charlotte J. Sumner
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-17

  • The AAA+ ATPase p97 protein is thought to be a potential anticancer target, but direct targeting on its ATPase function has not proven to be a successful strategy in clinical trials due to lack of selectivity. Here, the authors use biolayer interferometry-based fragment screening to identify ligands for the development of protein-protein interaction inhibitors by targeting the SHP-motif as a cofactor binding site in the N-domain of p97.

    • Sebastian Bothe
    • Petra Hänzelmann
    • Christoph Sotriffer
    ResearchOpen Access
    Communications Chemistry
    Volume: 5, P: 1-15

  • Junglas et al. probe into the mechanism of membrane stabilization by the inner membrane-associated protein of 30 kDa (IM30), a member of the phage shock protein A (PspA) family, and report that ring-shaped IM30 super-complexes disassemble upon binding to negatively charged membrane surfaces, involving partly unfolding of the monomers and formation of a membrane-protecting carpet. This study highlights the structural role of intrinsically disordered proteins in membrane stabilization.

    • Benedikt Junglas
    • Roberto Orru
    • Dirk Schneider
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-10