Structural basis of cell-cell adhesion by cadherins.
Crystal structures of the amino-terminal domain of N-cadherin provide a picture at the atomic level of a specific adhesive contact between cells. A repeated set of dimer interfaces is common to the structure in three lattices. These interactions combine to form a linear zipper of molecules that mirrors the linear structure of the intracellular filaments with which cadherins associate. This cell-adhesion zipper may provide a mechanism to marshal individual molecular adhesive interactions into strong bonds between cells.
Shapiro
L
L
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
Fannon
A M
AM
Kwong
P D
PD
Thompson
A
A
Lehmann
M S
MS
Grübel
G
G
Legrand
J F
JF
Als-Nielsen
J
J
Colman
D R
DR
Hendrickson
W A
WA
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D015820:Cadherins / Q000737:chemistry* / Q000502:physiology*; D002118:Calcium / Q000502:physiology; D002448:Cell Adhesion / Q000502:physiology*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins; D013329:Structure-Activity Relationship
D015820:Cadherins; D011993:Recombinant Fusion Proteins; D002118:Calcium