Solution structure of the epithelial cadherin domain responsible for selective cell adhesion.
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.
Overduin
M
M
Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.
Harvey
T S
TS
Bagby
S
S
Tong
K I
KI
Yau
P
P
Takeichi
M
M
Ikura
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D018801:CD2 Antigens / Q000737:chemistry; D015820:Cadherins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D002118:Calcium / Q000378:metabolism*; D002448:Cell Adhesion; D006860:Hydrogen Bonding; D007136:Immunoglobulins / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D018801:CD2 Antigens; D015820:Cadherins; D007136:Immunoglobulins; D002118:Calcium