ArticleJournal of molecular biology2008
Sequence and structural determinants of strand swapping in cadherin domains: do all cadherins bind through the same adhesive interface?
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 60 citations in OpenAlex.
- Ig or Not Ig? That Is the Question: The Nucleating Supersecondary Structure of the Ig-Fold and the Extended Ig Universe.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Review
- Antiparallel dimer structure of CELSR cadherin in solution revealed by high-speed atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Arrhythmogenic cardiomyopathy related DSG2 mutations affect desmosomal cadherin binding kinetics.Scientific reports · 2017Article
- Disruption of cell adhesion by an antibody targeting the cell-adhesive intermediate (X-dimer) of human P-cadherin.Scientific reports · 2017Article
- A Computational Model for Kinetic Studies of Cadherin Binding and Clustering.Biophysical journal · 2016Article
- Article
- Cadherin flexibility provides a key difference between desmosomes and adherens junctions.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Conservation weighting functions enable covariance analyses to detect functionally important amino acids.PloS one · 2014Article
- Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Origin of metazoan cadherin diversity and the antiquity of the classical cadherin/β-catenin complex.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Spontaneous dimerization of titin protein Z1Z2 domains induces strong nanomechanical anchoring.The Journal of biological chemistry · 2012Article
- Thinking outside the cell: how cadherins drive adhesion.Trends in cell biology · 2012Review
- Crystal structures of Drosophila N-cadherin ectodomain regions reveal a widely used class of Ca²+-free interdomain linkers.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Adherens junction assembly.Sub-cellular biochemistry · 2012Review
- Cross talk between focal adhesion kinase and cadherins: role in regulating endothelial barrier function.Microvascular research · 2012Review
- Cadherin selectivity filter regulates endothelial sieving properties.Nature communications · 2012Article
- Molecular design principles underlying β-strand swapping in the adhesive dimerization of cadherins.Nature structural & molecular biology · 2011Article
- Structure and binding mechanism of vascular endothelial cadherin: a divergent classical cadherin.Journal of molecular biology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Cadherins are cell surface adhesion proteins important for tissue development and integrity. Type I and type II, or classical, cadherins form adhesive dimers via an interface formed through the exchange, or "swapping", of the N-terminal beta-strands from their membrane-distal EC1 domains. Here, we ask which sequence and structural features in EC1 domains are responsible for beta-strand swapping and whether members of other cadherin families form similar strand-swapped binding interfaces. We created a comprehensive database of multiple alignments of each type of cadherin domain. We used the known three-dimensional structures of classical cadherins to identify conserved positions in multiple sequence alignments that appear to be crucial determinants of the cadherin domain structure. We identified features that are unique to EC1 domains. On the basis of our analysis, we conclude that all cadherin domains have very similar overall folds but, with the exception of classical and desmosomal cadherin EC1 domains, most of them do not appear to bind through a strand-swapping mechanism. Thus, non-classical cadherins that function in adhesion are likely to use different protein-protein interaction interfaces. Our results have implications for the evolution of molecular mechanisms of cadherin-mediated adhesion in vertebrates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.