ArticleJournal of molecular biology2007
The crystal structure of human E-cadherin domains 1 and 2, and comparison with other cadherins in the context of adhesion mechanism.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 130 citations in OpenAlex.
- Dual In Vivo and In Silico Exploration of Jet A‑1 Fuel Toxicity.ACS omega · 2026Article
- Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026Review
- Systematic Search for Blood-Brain Barrier Modulating Peptides Based on Exhaustive E-Cadherin Domain-Domain Docking.Journal of chemical information and modeling · 2025Article
- Strengthening E-cadherin adhesion via antibody-mediated binding stabilization.Structure (London, England : 1993) · 2024Article
- Mechanism of the blood-brain barrier modulation by cadherin peptides.Exploration of drug science · 2024Article
- Reversible photoregulation of cell-cell adhesions with opto-E-cadherin.Nature communications · 2023Article
- Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- Article
- 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
- Molecular mechanism underlying the increased risk of colorectal cancer metastasis caused by single nucleotide polymorphisms in LI-cadherin gene.Scientific reports · 2023Article
- Multiancestry genomic and transcriptomic analysis of gastric cancer.Nature genetics · 2023Article
- Transient interactions drive the lateral clustering of cadherin-23 on membrane.Communications biology · 2023Article
- Article
- Droplet Microarray Based Screening Identifies Proteins for Maintaining Pluripotency of hiPSCs.Advanced healthcare materials · 2022Article
- Molecular mechanism for strengthening E-cadherin adhesion using a monoclonal antibody.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multiple dimeric structures and strand-swap dimerization of E-cadherin in solution visualized by high-speed atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- E-Cadherin Signaling in Salivary Gland Development and Autoimmunity.Journal of clinical medicine · 2022Review
- Desmoglein 2 can undergo CaBiophysical journal · 2022Article
- A combined fragment-based virtual screening and STD-NMR approach for the identification of E-cadherin ligands.Frontiers in chemistry · 2022Article
- Heterophilic and homophilic cadherin interactions in intestinal intermicrovillar links are species dependent.PLoS biology · 2021Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Cell adhesion mediated by type I cadherins involves homophilic "trans" interactions that are thought to be brought about by a strand exchange mechanism involving the N-terminal extracellular domain. Here, we present the high-resolution crystal structure of the N-terminal two domains of human E-cadherin. Comparison of this structure with other type I cadherin structures reveals features that are likely to be critical to facilitate dimerization by strand exchange as well as dimer flexibility. We integrate this structural knowledge to provide a model for type I cadherin adhesive interactions. Intra-molecular docking of the conserved N-terminal "adhesion arm" into the acceptor pocket in monomeric E-cadherin appears largely identical to inter-molecular docking of the adhesion arm in adhesive trans dimers. A strained conformation of the adhesion arm in the monomer, however, may create an equilibrium between "open" and "closed" forms that primes the cadherin for formation of adhesive interactions, which are then stabilized by additional dimer-specific contacts. By contrast, in type II cadherins, strain in the adhesion arm appears absent and a much larger surface area is involved in trans adhesion, which may compensate the activation energy required to peel off the intra-molecularly docked arm. It seems that evolution has selected slightly different adhesion mechanisms for type I and type II cadherins.
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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.