title: The adhesive binding site of cadherins revisited.
abstract: Cadherins are single-pass transmembrane proteins that, through their homophilic specificity, function in selective cell adhesion and sorting. They have a modular structure that includes an ectodomain composed of tandem 'cadherin domains,' which have a beta-sandwich topology similar to that of immunoglobulin domains. Some early experiments suggest that, for the 'classical' cadherins, the adhesive specificity is encoded in the membrane-distal amino-terminal cadherin domain. Here, we review these data, and present new data that supports this idea.
authors.affiliation: Brookdale Center for Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York University, NY 10029, USA.
authors.forename: W S
authors.initials: WS
authors.lastname: Shan
authors.forename: A
authors.initials: A
authors.lastname: Koch
authors.forename: J
authors.initials: J
authors.lastname: Murray
authors.forename: D R
authors.initials: DR
authors.lastname: Colman
authors.forename: L
authors.initials: L
authors.lastname: Shapiro
mesh_terms: D000818:Animals; D001665:Binding Sites; D015820:Cadherins / Q000378:metabolism*; D002448:Cell Adhesion; D002449:Cell Aggregation; D002478:Cells, Cultured; D051379:Mice
chemical_list: D015820:Cadherins