{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670320287420800.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.1212912109"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.1212912109"}}],"dc:title":[{"@value":"Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell–cell adhesion"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>Nectins are members of the Ig superfamily that mediate cell–cell adhesion through homophilic and heterophilic interactions. We have determined the crystal structure of the nectin-2 homodimer at 1.3 Å resolution. Structural analysis and complementary mutagenesis studies reveal the basis for recognition and selectivity among the nectin family members. Notably, the close proximity of charged residues at the dimer interface is a major determinant of the binding affinities associated with homophilic and heterophilic interactions within the nectin family. Our structural and biochemical data provide a mechanistic basis to explain stronger heterophilic versus weaker homophilic interactions among these family members and also offer insights into nectin-mediated transinteractions between engaging cells.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380857613102804739","@type":"Researcher","foaf:name":[{"@value":"Dibyendu Samanta"}],"jpcoar:affiliationName":[{"@value":"Departments of aMicrobiology and Immunology,"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857613102804736","@type":"Researcher","foaf:name":[{"@value":"Udupi A. Ramagopal"}],"jpcoar:affiliationName":[{"@value":"Biochemistry,"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857613102804741","@type":"Researcher","foaf:name":[{"@value":"Rotem Rubinstein"}],"jpcoar:affiliationName":[{"@value":"Biochemistry,"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857613102804737","@type":"Researcher","foaf:name":[{"@value":"Vladimir Vigdorovich"}],"jpcoar:affiliationName":[{"@value":"Departments of aMicrobiology and Immunology,"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857613102804738","@type":"Researcher","foaf:name":[{"@value":"Stanley G. Nathenson"}],"jpcoar:affiliationName":[{"@value":"Departments of aMicrobiology and Immunology,"},{"@value":"Cell Biology, and"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857613102804740","@type":"Researcher","foaf:name":[{"@value":"Steven C. Almo"}],"jpcoar:affiliationName":[{"@value":"Biochemistry,"},{"@value":"Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"2012-08-27","prism:volume":"109","prism:number":"37","prism:startingPage":"14836","prism:endingPage":"14840"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.1212912109"}],"createdAt":"2012-08-28","modifiedAt":"2022-06-07","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050294045370104192","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Cellular recognition and patterning in sensory systems"}]},{"@id":"https://cir.nii.ac.jp/crid/1360005742494374528","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Aeromonas sobria serine protease decreases epithelial barrier function in T84 cells and accelerates bacterial translocation across the T84 monolayer in vitro"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283690752237184","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Nectins and Nectin-Like Molecules in Development and Disease"}]},{"@id":"https://cir.nii.ac.jp/crid/1360294643706513664","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Nectin-2 in general and in the brain"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846641849524736","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Nectin spot: a novel type of nectin-mediated cell adhesion apparatus"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1073/pnas.1212912109"},{"@type":"CROSSREF","@value":"10.1371/journal.pone.0221344_references_DOI_cDyLmcW42BaTUGEwatLV8x6VKf"},{"@type":"CROSSREF","@value":"10.1016/j.yexcr.2017.04.005_references_DOI_cDyLmcW42BaTUGEwatLV8x6VKf"},{"@type":"CROSSREF","@value":"10.1007/s11010-021-04241-y_references_DOI_cDyLmcW42BaTUGEwatLV8x6VKf"},{"@type":"CROSSREF","@value":"10.1042/bcj20160235_references_DOI_cDyLmcW42BaTUGEwatLV8x6VKf"},{"@type":"CROSSREF","@value":"10.1016/bs.ctdb.2014.11.019_references_DOI_cDyLmcW42BaTUGEwatLV8x6VKf"}]}