Cadherin-mediated cell-cell adhesion: sticking together as a family
- Resource Type
- Authors
- Chien Peter Chen; Saurabh D. Patel; Lawrence Shapiro; Fabiana Bahna; Barry Honig
- Source
- Current opinion in structural biology. 13(6)
- Subject
- Models, Molecular
Binding Sites
L1
Sequence Homology, Amino Acid
Cadherin
Cell adhesion molecule
Protein Conformation
Molecular Sequence Data
Adhesion
Biology
Cadherins
Transmembrane protein
Cell biology
Structure-Activity Relationship
Ectodomain
Structural Biology
Nectin
Cell Adhesion
Animals
Humans
Amino Acid Sequence
Cell adhesion
Molecular Biology
Protein Binding
Signal Transduction
- Language
- ISSN
- 0959-440X
The cadherins comprise a family of single-pass transmembrane proteins critical for cell-cell adhesion in vertebrates and invertebrates. The recently determined structure of the whole ectodomain from C-cadherin suggests that the adhesion of cadherins presented by juxtaposed cells is mediated by a strand-swapped dimer in which core hydrophobic elements are exchanged between the partner molecules. Sequence analysis suggests that several cadherin subfamilies share this adhesive mechanism. Recent work has shed new light on the molecular basis of cadherin adhesion, although understanding the specificity of these interactions remains a major challenge.