ArticleFrontiers in molecular biosciences2022
Role of TM3 in claudin-15 strand flexibility: A molecular dynamics study.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Molecular dynamics analyses of CLDN15 pore size and charge selectivity.The Journal of general physiology · 2026Article
- A multi-pore model of the blood-brain barrier tight junction strands recapitulates the permeability features of wild-type and mutant claudin-5.Protein science : a publication of the Protein Society · 2025Article
- Ion and water permeation through claudin-10b and claudin-15 paracellular channels.Computational and structural biotechnology journal · 2024Article
- Computational Models of Claudin Assembly in Tight Junctions and Strand Properties.International journal of molecular sciences · 2024Review
- Claudin-23 reshapes epithelial tight junction architecture to regulate barrier function.Nature communications · 2023Article
- The impact of pathogenic and artificial mutations on Claudin-5 selectivity from molecular dynamics simulations.Computational and structural biotechnology journal · 2023Article
- Multiscale modelling of claudin-based assemblies: A magnifying glass for novel structures of biological interfaces.Computational and structural biotechnology journal · 2022Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Claudins are cell-cell adhesion proteins within tight junctions that connect epithelial cells together. Claudins polymerize into a network of strand-like structures within the membrane of adjoining cells and create ion channels that control paracellular permeability to water and small molecules. Tight junction morphology and barrier function is tissue specific and regulated by claudin subtypes. Here, we present a molecular dynamics study of claudin-15 strands within lipid membranes and the role of a single-point mutation (A134P) on the third transmembrane helix (TM3) of claudin-15 in determining the morphology of the strand. Our results indicate that the A134P mutation significantly affects the lateral flexibility of the strands, increasing the persistence length of claudin-15 strands by a factor of three. Analyses of claudin-claudin contact in our
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