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Showing 1–4 of 4 results
Advanced filters: Author: Dawid Deneka Clear advanced filters

  • The structure of a homomeric channel of subunit A of leucine-rich repeat-containing protein 8 (LRRC8) determined by cryo-electron microscopy and X-ray crystallography reveals the basis for anion selectivity.

    • Dawid Deneka
    • Marta Sawicka
    • Raimund Dutzler
    Research
    Nature
    Volume: 558, P: 254-259

  • The human Tweety homologue (TTYH) family of transmembrane proteins have been suggested to act as chloride channels. Here the authors present cryo-EM structures of the 3 human TTYH paralogs that do not display the expected features of an anion channel, and instead appear to interact with lipid-like compounds residing in the membrane; suggesting an involvement in lipid-associated processes.

    • Anastasiia Sukalskaia
    • Monique S. Straub
    • Raimund Dutzler
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • The structure of a heteromeric volume-regulated LRRC8A/C channel shows a hexameric assembly of four clustered A subunits interspersed by two C subunits, which increase the mobility of the protein, thus facilitating channel activation.

    • Sonja Rutz
    • Dawid Deneka
    • Raimund Dutzler
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 52-61

  • Volume-regulated anion channels (VRACs) are heteromers of LRRC8 proteins, all containing the obligatory subunit LRRC8A. Here, the authors develop and characterize nanobodies that bind LRRC8A and allosterically modulate the function of homomeric LRRC8A and endogenous heteromeric channels, hinting at functional mechanisms present in VRACs.

    • Dawid Deneka
    • Sonja Rutz
    • Raimund Dutzler
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14