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Showing 1–6 of 6 results
Advanced filters: Author: Fabiana Bahna Clear advanced filters

  • Cryo-EM structures of the stabilized prefusion conformation of the glycoprotein B ectodomain—the HSV-1 entry machine—identify a prefusion-specific neutralizing antibody and reveal how prefusion glycoprotein B may evade antibody-mediated neutralization.

    • Ryan S. Roark
    • Andrew J. Schaub
    • Peter D. Kwong
    ResearchOpen Access
    Nature Microbiology
    Volume: 10, P: 2966-2980

  • Human and mouse astrocytes express the protocadherin PcdhγC3, which promotes self-recognition of individual astrocytes, thereby contributing to normal astrocyte and brain development.

    • John H. Lee
    • Alina P. Sergeeva
    • S. Lawrence Zipursky
    Research
    Nature
    Volume: 644, P: 164-172

  • The adhesive dimerization interface formed between cadherins involves the swapping of N-terminal β-strands between their EC1 domains. Molecular simulations, combined with biochemical and structural approaches, have unveiled the structural and energetic principles underlying the swapping process. These findings were used to confer strand-swapping properties on a naturally monomeric non-swapping cadherin domain.

    • Jeremie Vendome
    • Shoshana Posy
    • Barry Honig
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 693-700

  • Classical cadherins form two types of dimers: a strand swap version and an “X dimer” that lacks strand exchange between monomers. Strand swapping mutants are now found to form the X-dimer structure. Together with further experiments, this supports the idea that the X-dimer is an intermediate configuration that promotes strand swapped dimer formation.

    • Oliver J Harrison
    • Fabiana Bahna
    • Lawrence Shapiro
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 348-357

  • T-cadherin is a non-classical GPI-anchored cadherin. The crystal structures of T-cadherins from different organisms now reveal that the EC1-EC2 regions can form dimers via an interface near the EC1-EC2 calcium binding sites, different from the EC1 strand swapping seen in classical cadherin homophilic interactions.

    • Carlo Ciatto
    • Fabiana Bahna
    • Lawrence Shapiro
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 339-347

  • Clustered protocadherin ectodomains spontaneously assemble to form a zipper-like lattice of alternating cis and trans interactions at membrane contact sites, which probably represents their mode of function in neuronal self-recognition.

    • Julia Brasch
    • Kerry M. Goodman
    • Lawrence Shapiro
    Research
    Nature
    Volume: 569, P: 280-283