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Showing 1–8 of 8 results
Advanced filters: Author: Michelle A. Dunstone Clear advanced filters

  • The membrane attack complex is a heteromeric assembly of complement proteins where multiple copies of C9 are recruited by the C5b678 complex to form lytic pores in pathogen membranes. Here the authors present the structure of a soluble pore-like form of the C9 component that reveals details of the oligomerization interfaces.

    • Natalya V. Dudkina
    • Bradley A. Spicer
    • Michelle A. Dunstone
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-6

  • Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors present structures of hexadecameric MPEG1 prepores both in solution and in complex with liposomes.

    • Siew Siew Pang
    • Charles Bayly-Jones
    • James C. Whisstock
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9

  • The Complement component 9 (C9) is the pore-forming component of the Membrane Attack Complex which targets pathogens. Here authors use structural biology to compare monomeric C9 to C9 within the polymeric assembly and identify the element which inhibits C9 self-assembly in the absence of the target membrane.

    • Bradley A. Spicer
    • Ruby H. P. Law
    • Michelle A. Dunstone
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-7

  • Cryo-EM, crystallography, biochemical experiments and computational approaches have been used to study different intermediate states of the Aeromonas hydrophila toxin aerolysin en route to pore formation. These results reveal that an unexpected and marked rotation of the core aerolysin machinery is required to unleash the membrane-spanning regions.

    • James C Whisstock
    • Michelle A Dunstone
    News & Views
    Nature Chemical Biology
    Volume: 9, P: 605-606

  • Perforin monomers self-assemble into pre-pores that first insert into the membrane and then recruit additional subunits to grow in size.

    • Carl Leung
    • Adrian W. Hodel
    • Bart W. Hoogenboom
    Research
    Nature Nanotechnology
    Volume: 12, P: 467-473

  • Natural killer cells and cytotoxic T cells kill virus-infected and malignant cells, releasing the pore-forming protein perforin in the process. Perforin is required for the delivery of pro-apoptotic granzymes to the target cell. These authors present the crystal structure of a perforin monomer together with a cryo-electron microscopy reconstruction of the oligomeric pore. Perforin monomers within the pore are arranged with an inside-out orientation relative to the structurally homologous monomers of cholesterol-dependent cytolysins.

    • Ruby H. P. Law
    • Natalya Lukoyanova
    • James C. Whisstock
    Research
    Nature
    Volume: 468, P: 447-451