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Showing 1–6 of 6 results
Advanced filters: Author: Julia Brasch Clear advanced filters

  • 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

  • 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

  • Nectins and nectin-like proteins promote intercellular adhesion and tissue patterning in vertebrates through homophilic or heterophilic interactions. Now the formation of all the possible nectin pairs is studied systematically in vitro, and crystal structures provide insight into the molecular basis for the adhesive binding specificity of nectins.

    • Oliver J Harrison
    • Jeremie Vendome
    • Lawrence Shapiro
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 906-915

  • 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