ArticleThe Journal of biological chemistry2011
Crystal Structure of the cis-Dimer of Nectin-1: implications for the architecture of cell-cell junctions.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- Prime editing of Nectin-1 functional domains confers knockout-level resistance to pseudorabies virus.BMC veterinary research · 2026Article
- Placental transcriptome profiling in congenital Chagas disease: gene networks associated with transmission.Frontiers in cellular and infection microbiology · 2026Article
- Rare missense variants inFrontiers in genetics · 2026Article
- Breaching the Barrier: Investigating Initial Herpes Simplex Viral Infection and Spread in Human Skin and Mucosa.Viruses · 2024Review
- SynCAMs in Normal Vertebrate Neural Development and Neuropsychiatric Disorders: from the Perspective of the OCAs.Molecular neurobiology · 2024Review
- Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Review
- Review
- Tracing the evolution of nectin and nectin-like cell adhesion molecules.Scientific reports · 2020Article
- Structural basis for the dominant or recessive character of GLIALCAM mutations found in leukodystrophies.Human molecular genetics · 2020Article
- Adhesion Protein Structure, Molecular Affinities, and Principles of Cell-Cell Recognition.Cell · 2020Review
- Inactivating mutations and X-ray crystal structure of the tumor suppressor OPCML reveal cancer-associated functions.Nature communications · 2019Article
- Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior.Cell reports · 2018Article
- Junctional adhesion molecule-A: functional diversity through molecular promiscuity.Cellular and molecular life sciences : CMLS · 2018Review
- Structural, mutational and biophysical studies reveal a canonical mode of molecular recognition between immune receptor TIGIT and nectin-2.Molecular immunology · 2017Article
- Promoter-Specific Expression and Genomic Structure of IgLON Family Genes in Mouse.Frontiers in neuroscience · 2017Article
- Article
- Crystal structure of afadin PDZ domain-nectin-3 complex shows the structural plasticity of the ligand-binding site.Protein science : a publication of the Protein Society · 2015Article
- Nectin family of cell-adhesion molecules: structural and molecular aspects of function and specificity.Cellular and molecular life sciences : CMLS · 2015Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In multicellular organisms, cells are interconnected by cell adhesion molecules. Nectins are immunoglobulin (Ig)-like cell adhesion molecules that mediate homotypic and heterotypic cell-cell adhesion, playing key roles in tissue organization. To mediate cell-cell adhesion, nectin molecules dimerize in cis on the surface of the same cell, followed by trans-dimerization of the cis-dimers between the neighboring cells. Previous cell biological studies deduced that the first Ig-like domain of nectin and the second Ig-like domain are involved in trans-dimerization and cis-dimerization, respectively. However, to understand better the steps involved in nectin adhesion, the structural basis for the dimerization of nectin must be determined. In this study, we determined the first crystal structure of the entire extracellular region of nectin-1. In the crystal, nectin-1 formed a V-shaped homophilic dimer through the first Ig-like domain. Structure-based site-directed mutagenesis of the first Ig-like domain identified four essential residues that are involved in the homophilic dimerization. Upon mutating the four residues, nectin-1 significantly decreased cis-dimerization on the surface of cultured cells and abolished the homophilic and heterophilic adhesion activities. These results indicate that, in contrast with the previous notion, our structure represents a cis-dimer. Thus, our findings clearly reveal the structural basis for the cis-dimerization of nectins through the first Ig-like domains.
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