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Showing 1–11 of 11 results
Advanced filters: Author: Samir Benlekbir Clear advanced filters

  • Authors present the structure of Ycf1p, a homolog of multidrug resistance protein 1 (MRP1). The monomeric and dimeric Ycf1p species are differentially phosphorylated and possess different ATPase activities indicating that dimerization affects the function of the protein.

    • Sarah C. Bickers
    • Samir Benlekbir
    • Voula Kanelis
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15

  • Here, the authors combine three different antibody specificities and an Fc domain on a single multivalent molecule, resulting in high neutralization activity despite viral sequence variability.

    • Edurne Rujas
    • Iga Kucharska
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Structural insights into the small heat shock proteins (sHsps) complexes with their substrates are sparse. Here, cryo-EM structure of a plastid sHsp, Hsp21, in complex with a bona fide substrate 1-deoxy-D-xylulose 5-phosphate synthase (DXPS), suggests the anti-aggregation mechanism employed by sHsps.

    • Chuanyang Yu
    • Stephen King Pong Leung
    • Wilson Chun Yu Lau
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-11

  • A cryo-electron microscopy structure of the DNA damage repair protein 53BP1 bound to a nucleosome illuminates the way 53BP1 recognizes two types of histone modifications (a methyl group and a ubiquitin moiety), and provides insight into the highly specified recognition and recruitment of 53BP1 to modified chromatin.

    • Marcus D. Wilson
    • Samir Benlekbir
    • Daniel Durocher
    Research
    Nature
    Volume: 536, P: 100-103

  • Vacuolar-type ATPases (V-type ATPases) are large integral membrane protein complexes. Their activity acidifies intracellular compartments, and they are regulated by the dissociation of the complex's V1 and VO regions. The cryo-EM reconstruction of the yeast V-type ATPase suggests how structural rearrangements triggered by dissociation of V1 leads to inhibition of activity.

    • Samir Benlekbir
    • Stephanie A Bueler
    • John L Rubinstein
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 1356-1362

  • Bacterial type IV pilus-like systems catalyse the formation of pilin fibres but it is unknown how they are powered. Here, the authors present crystal and cryo-EM structures of the hexameric motor ATPases PilB and PilT from Type IVa Pilus that reveal different conformational states, classify the conformations of all PilT-like ATPase structures and propose a model for PilT function.

    • Matthew McCallum
    • Samir Benlekbir
    • P. Lynne Howell
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-16

  • The B-cell-specific co-receptor CD22 is a therapeutic target for depleting dysregulated B cells. Here the authors structurally characterize the ectodomain of CD22 and present its crystal structure with the bound therapeutic antibody epratuzumab, which gives insights into the mechanism of inhibition of B-cell activation.

    • June Ereño-Orbea
    • Taylor Sicard
    • Jean-Philippe Julien
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • The structure of the VO subcomplex of yeast V-ATPase, solved by electron cryomicroscopy, reveals a new subunit and suggests a mechanism for the translocation of protons across membranes.

    • Mohammad T. Mazhab-Jafari
    • Alexis Rohou
    • John L. Rubinstein
    Research
    Nature
    Volume: 539, P: 118-122