Solution structure of the epithelial cadherin domain responsible for selective cell adhesion
Science, 1995•science.org
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 α helix and by
loops at one end of the seven-stranded β-barrel structure. An exposed concave face is in a
position to provide homophilic binding specificity and was also sensitive to calcium ligation …
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 α helix and by
loops at one end of the seven-stranded β-barrel structure. An exposed concave face is in a
position to provide homophilic binding specificity and was also sensitive to calcium ligation …
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 α helix and by loops at one end of the seven-stranded β-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.
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