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Showing 1–8 of 8 results
Advanced filters: Author: Jeremie Vendome Clear advanced filters

  • 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

  • Structural, functional and in silico analyses of the chloroquine-resistance transporter PfCRT of Plasmodium falciparum suggest that distinct mechanistic features mediate the resistance to chloroquine and piperaquine in drug-resistant parasites.

    • Jonathan Kim
    • Yong Zi Tan
    • Filippo Mancia
    Research
    Nature
    Volume: 576, P: 315-320

  • The subtilisin-like domain of PatG can catalyze the macrocyclization of linear peptide. The crystal structure of the PatG macrocyclase domain, along with mutagenesis and functional analyses, reveals how the enzyme recognizes its substrate and enforces macrocyclization over hydrolysis of the acyl-enzyme intermediate. This information is also used to engineer variants with altered specificity and enhanced catalytic activity.

    • Jesko Koehnke
    • Andrew Bent
    • James H Naismith
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 767-772

  • 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