Crystal structures of the amino-terminal domain of N-cadherin provide
a picture at the atomic level of a specific adhesive contact between c
ells. 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 fila
ments with which cadherins associate. This cell-adhesion zipper may pr
ovide a mechanism to marshal individual molecular adhesive interaction
s into strong bonds between cells.