Solution structure of the epithelial cadherin domain responsible for selective cell adhesion

Science. 1995 Jan 20;267(5196):386-9. doi: 10.1126/science.7824937.


Cadherins are calcium-dependent cell adhesion molecules containing extracellular repeats of approximately 110 amino acids. The three-dimensional structure of the amino-terminal repeat of mouse epithelial cadherin was determined by multidimensional heteronuclear magnetic resonance spectroscopy. The calcium ion was bound by a short alpha helix and by loops at one end of the seven-stranded beta-barrel structure. An exposed concave face is in a position to provide homophilic binding specificity and was also sensitive to calcium ligation. Unexpected structural similarities with the immunoglobulin fold suggest an evolutionary relation between calcium-dependent and calcium-independent cell adhesion molecules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CD2 Antigens / chemistry
  • Cadherins / chemistry*
  • Cadherins / metabolism
  • Cadherins / physiology
  • Calcium / metabolism*
  • Cell Adhesion*
  • Hydrogen Bonding
  • Immunoglobulins / chemistry
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary


  • CD2 Antigens
  • Cadherins
  • Immunoglobulins
  • Calcium